Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Science 9 December 1994:
Vol. 266. no. 5191, pp. 1669 - 1674
DOI: 10.1126/science.7992050
Prev | Table of Contents | Next

Articles

Science, Vol 266, Issue 5191, 1669-1674
Copyright © 1994 by American Association for the Advancement of Science

articles

How a protein binds B12: A 3.0 A X-ray structure of B12-binding domains of methionine synthase

CL Drennan, S Huang, JT Drummond, RG Matthews, and ML Lidwig

Biophysics Research Division, University of Michigan, Ann Arbor 48109-1055.

The crystal structure of a 27-kilodalton methylcobalamin-containing fragment of methionine synthase from Escherichia coli was determined at 3.0 A resolution. This structure depicts cobalamin-protein interactions and reveals that the corrin macrocycle lies between a helical amino-terminal domain and an alpha/beta carboxyl-terminal domain that is a variant of the Rossmann fold. Methylcobalamin undergoes a conformational change on binding the protein; the dimethylbenzimidazole group, which is coordinated to the cobalt in the free cofactor, moves away from the corrin and is replaced by a histidine contributed by the protein. The sequence Asp-X-His-X-X-Gly, which contains this histidine ligand, is conserved in the adenosylcobalamin-dependent enzymes methylmalonyl-coenzyme A mutase and glutamate mutase, suggesting that displacement of the dimethylbenzimidazole will be a feature common to many cobalamin-binding proteins. Thus the cobalt ligand, His759, and the neighboring residues Asp757 and Ser810, may form a catalytic quartet, Co-His-Asp-Ser, that modulates the reactivity of the B12 prosthetic group in methionine synthase.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Insights into the reactivation of cobalamin-dependent methionine synthase.
M. Koutmos, S. Datta, K. A. Pattridge, J. L. Smith, and R. G. Matthews (2009)
PNAS 106, 18527-18532
   Abstract »    Full Text »    PDF »
A Love Affair with Vitamins.
R. G. Matthews (2009)
J. Biol. Chem. 284, 26217-26228
   Full Text »    PDF »
RamA, a Protein Required for Reductive Activation of Corrinoid-dependent Methylamine Methyltransferase Reactions in Methanogenic Archaea.
T. Ferguson, J. A. Soares, T. Lienard, G. Gottschalk, and J. A. Krzycki (2009)
J. Biol. Chem. 284, 2285-2295
   Abstract »    Full Text »    PDF »
The Ether-Cleaving Methyltransferase System of the Strict Anaerobe Acetobacterium dehalogenans: Analysis and Expression of the Encoding Genes.
A. Schilhabel, S. Studenik, M. Vodisch, S. Kreher, B. Schlott, A. Y. Pierik, and G. Diekert (2009)
J. Bacteriol. 191, 588-599
   Abstract »    Full Text »    PDF »
Decyanation of vitamin B12 by a trafficking chaperone.
J. Kim, C. Gherasim, and R. Banerjee (2008)
PNAS 105, 14551-14554
   Abstract »    Full Text »    PDF »
Gene Identification for the cblD Defect of Vitamin B12 Metabolism.
D. Coelho, T. Suormala, M. Stucki, J. P. Lerner-Ellis, D. S. Rosenblatt, R. F. Newbold, M. R. Baumgartner, and B. Fowler (2008)
N. Engl. J. Med. 358, 1454-1464
   Abstract »    Full Text »    PDF »
A disulfide-stabilized conformer of methionine synthase reveals an unexpected role for the histidine ligand of the cobalamin cofactor.
S. Datta, M. Koutmos, K. A. Pattridge, M. L. Ludwig, and R. G. Matthews (2008)
PNAS 105, 4115-4120
   Abstract »    Full Text »    PDF »
The CbiB Protein of Salmonella enterica Is an Integral Membrane Protein Involved in the Last Step of the De Novo Corrin Ring Biosynthetic Pathway.
C. L. Zayas, K. Claas, and J. C. Escalante-Semerena (2007)
J. Bacteriol. 189, 7697-7708
   Abstract »    Full Text »    PDF »
Crystal structure of human intrinsic factor: Cobalamin complex at 2.6-A resolution.
F. S. Mathews, M. M. Gordon, Z. Chen, K. R. Rajashankar, S. E. Ealick, D. H. Alpers, and N. Sukumar (2007)
PNAS 104, 17311-17316
   Abstract »    Full Text »    PDF »
Insight into the mechanism of biological methanol activation based on the crystal structure of the methanol-cobalamin methyltransferase complex.
C. H. Hagemeier, M. Krer, R. K. Thauer, E. Warkentin, and U. Ermler (2006)
PNAS 103, 18917-18922
   Abstract »    Full Text »    PDF »
Structural insights into methyltransfer reactions of a corrinoid iron-sulfur protein involved in acetyl-CoA synthesis.
T. Svetlitchnaia, V. Svetlitchnyi, O. Meyer, and H. Dobbek (2006)
PNAS 103, 14331-14336
   Abstract »    Full Text »    PDF »
Human methionine synthase reductase is a molecular chaperone for human methionine synthase.
K. Yamada, R. A. Gravel, T. Toraya, and R. G. Matthews (2006)
PNAS 103, 9476-9481
   Abstract »    Full Text »    PDF »
Structural basis for mammalian vitamin B12 transport by transcobalamin.
J. Wuerges, G. Garau, S. Geremia, S. N. Fedosov, T. E. Petersen, and L. Randaccio (2006)
PNAS 103, 4386-4391
   Abstract »    Full Text »    PDF »
The Residue Mass of L-Pyrrolysine in Three Distinct Methylamine Methyltransferases.
J. A. Soares, L. Zhang, R. L. Pitsch, N. M. Kleinholz, R. B. Jones, J. J. Wolff, J. Amster, K. B. Green-Church, and J. A. Krzycki (2005)
J. Biol. Chem. 280, 36962-36969
   Abstract »    Full Text »    PDF »
Identification and Characterization of a Novel Vitamin B12 (Cobalamin) Biosynthetic Enzyme (CobZ) from Rhodobacter capsulatus, Containing Flavin, Heme, and Fe-S Cofactors.
H. M. McGoldrick, C. A. Roessner, E. Raux, A. D. Lawrence, K. J. McLean, A. W. Munro, S. Santabarbara, S. E. J. Rigby, P. Heathcote, A. I. Scott, et al. (2005)
J. Biol. Chem. 280, 1086-1094
   Abstract »    Full Text »    PDF »
A locking mechanism preventing radical damage in the absence of substrate, as revealed by the x-ray structure of lysine 5,6-aminomutase.
F. Berkovitch, E. Behshad, K.-H. Tang, E. A. Enns, P. A. Frey, and C. L. Drennan (2004)
PNAS 101, 15870-15875
   Abstract »    Full Text »    PDF »
The N Terminus of Myxococcus xanthus CarA Repressor Is an Autonomously Folding Domain That Mediates Physical and Functional Interactions with Both Operator DNA and Antirepressor Protein.
M. C. Perez-Marin, J. J. Lopez-Rubio, F. J. Murillo, M. Elias-Arnanz, and S. Padmanabhan (2004)
J. Biol. Chem. 279, 33093-33103
   Abstract »    Full Text »    PDF »
Purification, Cloning, and Sequencing of a 3,5-Dichlorophenol Reductive Dehalogenase from Desulfitobacterium frappieri PCP-1.
J. Thibodeau, A. Gauthier, M. Duguay, R. Villemur, F. Lepine, P. Juteau, and R. Beaudet (2004)
Appl. Envir. Microbiol. 70, 4532-4537
   Abstract »    Full Text »    PDF »
Inaugural Article: Biography of Martha L. Ludwig.
E. Hitt (2004)
PNAS 101, 3727-3728
   Full Text »    PDF »
Inaugural Article: Structures of the N-terminal modules imply large domain motions during catalysis by methionine synthase.
J. C. Evans, D. P. Huddler, M. T. Hilgers, G. Romanchuk, R. G. Matthews, and M. L. Ludwig (2004)
PNAS 101, 3729-3736
   Abstract »    Full Text »    PDF »
Natural selection of more designable folds: A mechanism for thermophilic adaptation.
J. L. England, B. E. Shakhnovich, and E. I. Shakhnovich (2003)
PNAS 100, 8727-8731
   Abstract »    Full Text »    PDF »
Inaugural Article: Factors modulating conformational equilibria in large modular proteins: A case study with cobalamin-dependent methionine synthase.
V. Bandarian, M. L. Ludwig, and R. G. Matthews (2003)
PNAS 100, 8156-8163
   Abstract »    Full Text »    PDF »
Identification of the Human and Bovine ATP:Cob(I)alamin Adenosyltransferase cDNAs Based on Complementation of a Bacterial Mutant.
N. A. Leal, S. D. Park, P. E. Kima, and T. A. Bobik (2003)
J. Biol. Chem. 278, 9227-9234
   Abstract »    Full Text »    PDF »
Crystal Structures of the BtuF Periplasmic-binding Protein for Vitamin B12 Suggest a Functionally Important Reduction in Protein Mobility upon Ligand Binding.
N. K. Karpowich, H. H. Huang, P. C. Smith, and J. F. Hunt (2003)
J. Biol. Chem. 278, 8429-8434
   Abstract »    Full Text »    PDF »
Identification and in vivo characterization of PpaA, a regulator of photosystem formation in Rhodobacter sphaeroides.
L. Gomelsky, J. Sram, O. V. Moskvin, I. M. Horne, H. N. Dodd, J. M. Pemberton, A. G. McEwan, S. Kaplan, and M. Gomelsky (2003)
Microbiology 149, 377-388
   Abstract »    Full Text »    PDF »
The structure of Escherichia coli BtuF and binding to its cognate ATP binding cassette transporter.
E. L. Borths, K. P. Locher, A. T. Lee, and D. C. Rees (2002)
PNAS 99, 16642-16647
   Abstract »    Full Text »    PDF »
A New UAG-Encoded Residue in the Structure of a Methanogen Methyltransferase.
B. Hao, W. Gong, T. K. Ferguson, C. M. James, J. A. Krzycki, and M. K. Chan (2002)
Science 296, 1462-1466
   Abstract »    Full Text »    PDF »
Importance of the Histidine Ligand to Coenzyme B12 in the Reaction Catalyzed by Methylmalonyl-CoA Mutase.
M. Vlasie, S. Chowdhury, and R. Banerjee (2002)
J. Biol. Chem. 277, 18523-18527
   Abstract »    Full Text »    PDF »
Functional vitamin B12 deficiency and Alzheimer disease.
A. McCaddon, B. Regland, P. Hudson, and G. Davies (2002)
Neurology 58, 1395-1399
   Abstract »    Full Text »    PDF »
Role for Vitamin B12 in Light Induction of Gene Expression in the Bacterium Myxococcus xanthus.
M. Cervantes and F. J. Murillo (2002)
J. Bacteriol. 184, 2215-2224
   Abstract »    Full Text »    PDF »
MeaA, a Putative Coenzyme B12-Dependent Mutase, Provides Methylmalonyl Coenzyme A for Monensin Biosynthesis in Streptomyces cinnamonensis.
W. Zhang and K. A. Reynolds (2001)
J. Bacteriol. 183, 2071-2080
   Abstract »    Full Text »    PDF »
Chloromethane Utilization Gene Cluster from Hyphomicrobium chloromethanicum Strain CM2T and Development of Functional Gene Probes To Detect Halomethane-Degrading Bacteria.
C. McAnulla, C. A. Woodall, I. R. McDonald, A. Studer, S. Vuilleumier, T. Leisinger, and J. C. Murrell (2001)
Appl. Envir. Microbiol. 67, 307-316
   Abstract »    Full Text »    PDF »
Native Corrinoids from Clostridium cochlearium Are Adeninylcobamides: Spectroscopic Analysis and Identification of Pseudovitamin B12 and Factor A.
B. Hoffmann, M. Oberhuber, E. Stupperich, H. Bothe, W. Buckel, R. Konrat, and B. Krautler (2000)
J. Bacteriol. 182, 4773-4782
   Abstract »    Full Text »    PDF »
The Trimethylamine Methyltransferase Gene and Multiple Dimethylamine Methyltransferase Genes of Methanosarcina barkeri Contain In-Frame and Read-Through Amber Codons.
L. Paul, D. J. Ferguson Jr., and J. A. Krzycki (2000)
J. Bacteriol. 182, 2520-2529
   Abstract »    Full Text »    PDF »
Heterologous High Level Expression, Purification, and Enzymological Properties of Recombinant Rat Cobalamin-dependent Methionine Synthase.
K. Yamada, S. Yamada, T. Tobimatsu, and T. Toraya (1999)
J. Biol. Chem. 274, 35571-35576
   Abstract »    Full Text »    PDF »
Cloning and Sequencing of the Coenzyme B12-binding Domain of Isobutyryl-CoA Mutase from Streptomyces cinnamonensis, Reconstitution of Mutase Activity, and Characterization of the Recombinant Enzyme Produced in Escherichia coli.
A. Ratnatilleke, J. W. Vrijbloed, and J. A. Robinson (1999)
J. Biol. Chem. 274, 31679-31685
   Abstract »    Full Text »    PDF »
A Polymorphism of the Methionine Synthase Gene: Association with Plasma Folate, Vitamin B12, Homocyst(e)ine, and Colorectal Cancer Risk.
J. Ma, M. J. Stampfer, B. Christensen, E. Giovannucci, D. J. Hunter, J. Chen, W. C. Willett, J. Selhub, C. H. Hennekens, R. Gravel, et al. (1999)
Cancer Epidemiol. Biomarkers Prev. 8, 825-829
   Abstract »    Full Text »
A corrinoid-dependent catabolic pathway for growth of a Methylobacterium strain with chloromethane.
T. Vannelli, M. Messmer, A. Studer, S. Vuilleumier, and T. Leisinger (1999)
PNAS 96, 4615-4620
   Abstract »    Full Text »    PDF »
Binding of Cob(II)alamin to the Adenosylcobalamin-dependent Ribonucleotide Reductase from Lactobacillus leichmannii. IDENTIFICATION OF DIMETHYLBENZIMIDAZOLE AS THE AXIAL LIGAND.
C. C. Lawrence, G. J. Gerfen, V. Samano, R. Nitsche, M. J. Robins, J. Retey, and J. Stubbe (1999)
J. Biol. Chem. 274, 7039-7042
   Abstract »    Full Text »    PDF »
Clustered Genes Encoding the Methyltransferases of Methanogenesis from Monomethylamine.
S. A. Burke, S. L. Lo, and J. A. Krzycki (1998)
J. Bacteriol. 180, 3432-3440
   Abstract »    Full Text »    PDF »
Cloning and mapping of a cDNA for methionine synthase reductase, a flavoprotein defective in patients with homocystinuria.
D. Leclerc, A. Wilson, R. Dumas, C. Gafuik, D. Song, D. Watkins, H. H. Q. Heng, J. M. Rommens, S. W. Scherer, D. S. Rosenblatt, et al. (1998)
PNAS 95, 3059-3064
   Abstract »    Full Text »    PDF »
Cloning, Sequencing, Expression, and Insertional Inactivation of the Gene for the Large Subunit of the Coenzyme B12-dependent Isobutyryl-CoA Mutase from Streptomyces cinnamonensis.
K. Zerbe-Burkhardt, A. Ratnatilleke, N. Philippon, A. Birch, A. Leiser, J. W. Vrijbloed, D. Hess, P. Hunziker, and J. A. Robinson (1998)
J. Biol. Chem. 273, 6508-6517
   Abstract »    Full Text »    PDF »
Solid and liquid phase 59Co NMR studies of cobalamins and their derivatives.
A. Medek, V. Frydman, and L. Frydman (1997)
PNAS 94, 14237-14242
   Abstract »    Full Text »    PDF »
Homocysteine as a Risk Factor for Vascular Disease : Enhanced Collagen Production and Accumulation by Smooth Muscle Cells.
A. Majors, L. A. Ehrhart, and E. H. Pezacka (1997)
Arterioscler Thromb Vasc Biol 17, 2074-2081
   Abstract »    Full Text »
Reconstitution of Monomethylamine:Coenzyme M Methyl Transfer with a Corrinoid Protein and Two Methyltransferases Purified from Methanosarcina barkeri.
S. A. Burke and J. A. Krzycki (1997)
J. Biol. Chem. 272, 16570-16577
   Abstract »    Full Text »    PDF »
Human Methionine Synthase. cDNA CLONING, GENE LOCALIZATION, AND EXPRESSION.
L. H. Chen, M.-L. Liu, H.-Y. Hwang, L.-S. Chen, J. Korenberg, and B. Shane (1997)
J. Biol. Chem. 272, 3628-3634
   Abstract »    Full Text »    PDF »
The B12-dependent ribonucleotide reductase from the archaebacterium Thermoplasma acidophila: An evolutionary solution to the ribonucleotide reductase conundrum.
A. Tauer and S. A. Benner (1997)
PNAS 94, 53-58
   Abstract »    Full Text »    PDF »
Carboxymethylation of MutS-Cysteine-15 Specifically Inactivates Adenosylcobalamin-dependent Glutamate Mutase. EXAMINATION OF THE ROLE OF THIS RESIDUE IN COENZYME-BINDING AND CATALYSIS.
D. E. Holloway, H.-P. Chen, and E. N. G. Marsh (1996)
J. Biol. Chem. 271, 29121-29125
   Abstract »    Full Text »    PDF »
Cloning, Sequencing, and High Level Expression of the Genes Encoding Adenosylcobalamin-dependent Glycerol Dehydrase of Klebsiella pneumoniae.
T. Tobimatsu, M. Azuma, H. Matsubara, H. Takatori, T. Niida, K. Nishimoto, H. Satoh, R. Hayashi, and T. Toraya (1996)
J. Biol. Chem. 271, 22352-22357
   Abstract »    Full Text »    PDF »
Binding site revealed of nature's most beautiful cofactor.
J Stubbe (1994)
Science 266, 1663-1664
   PDF »
The Coenzyme B12 Analog 5'-Deoxyadenosylcobinamide-GDP Supports Catalysis by Methylmalonyl-CoA Mutase in the Absence of Trans-ligand Coordination.
S. Chowdhury, M. G. Thomas, J. C. Escalante-Semerena, and R. Banerjee (2001)
J. Biol. Chem. 276, 1015-1019
   Abstract »    Full Text »    PDF »
The MtsA Subunit of the Methylthiol:Coenzyme M Methyltransferase of Methanosarcina barkeri Catalyses Both Half-reactions of Corrinoid-dependent Dimethylsulfide: Coenzyme M Methyl Transfer.
T. C. Tallant, L. Paul, and J. A. Krzycki (2001)
J. Biol. Chem. 276, 4485-4493
   Abstract »    Full Text »    PDF »
Structural Investigation of the Biosynthesis of Alternative Lower Ligands for Cobamides by Nicotinate Mononucleotide: 5,6-Dimethylbenzimidazole Phosphoribosyltransferase from Salmonella enterica.
C.-G. Cheong, J. C. Escalante-Semerena, and I. Rayment (2001)
J. Biol. Chem. 276, 37612-37620
   Abstract »    Full Text »    PDF »
Cloning, Sequencing, Heterologous Expression, Purification, and Characterization of Adenosylcobalamin-dependent D-Ornithine Aminomutase from Clostridium sticklandii.
H.-P. Chen, S.-H. Wu, Y.-L. Lin, C.-M. Chen, and S.-S. Tsay (2001)
J. Biol. Chem. 276, 44744-44750
   Abstract »    Full Text »    PDF »
Reconstitution of Dimethylamine:Coenzyme M Methyl Transfer with a Discrete Corrinoid Protein and Two Methyltransferases Purified from Methanosarcina barkeri.
D. J. Ferguson Jr., N. Gorlatova, D. A. Grahame, and J. A. Krzycki (2000)
J. Biol. Chem. 275, 29053-29060
   Abstract »    Full Text »    PDF »
Mapping the interactions between flavodoxin and its physiological partners flavodoxin reductase and cobalamin-dependent methionine synthase.
D. A. Hall, C. W. Vander Kooi, C. N. Stasik, S. Y. Stevens, E. R. P. Zuiderweg, and R. G. Matthews (2001)
PNAS 98, 9521-9526
   Abstract »    Full Text »    PDF »


To Advertise     Find Products

Science. ISSN 0036-8075 (print), 1095-9203 (online)