Related Content
Search Google Scholar for:
|
|
Science 2 December 1988:
Vol. 242. no. 4883, pp. 1290 - 1295
DOI: 10.1126/science.3057628
|
|
Articles
Science, Vol 242, Issue 4883, 1290-1295
Copyright © 1988 by American Association for the Advancement of Science
Sugar and signal-transducer binding sites of the Escherichia coli galactose chemoreceptor protein
NK Vyas,
MN Vyas,
and
FA Quiocho
Howard Hughes Medical Institute, Baylor College of Medicine, Houston, TX 77030.
D-galactose-binding (or chemoreceptor) protein of Escherichia coli serves as an initial component for both chemotaxis towards galactose and glucose and high-affinity active transport of the two sugars. Well-refined x-ray structures of the liganded forms of the wild-type and a mutant protein isolated from a strain defective in chemotaxis but fully competent in transport have provided a molecular view of the sugar-binding site and of a site for interacting with the Trg transmembrane signal transducer. The geometry of the sugar-binding site, located in the cleft between the two lobes of the bilobate protein, is novel in that it is designed for tight binding and sequestering of either the alpha or beta anomer of the D-stereoisomer of the 4-epimers galactose and glucose. Binding specificity and affinity are conferred primarily by polar planar side-chain residues that form intricate networks of cooperative and bidentate hydrogen bonds with the sugar substrates, and secondarily by aromatic residues that sandwich the pyranose ring. Each of the pairs of anomeric hydroxyls and epimeric hydroxyls is recognized by a distinct Asp residue. The site for interaction with the transducer is about 18 A from the sugar-binding site. Mutation of Gly74 to Asp at this site, concomitant with considerable changes in the local ordered water structures, contributes to the lack of productive interaction with the transmembrane signal transducer.
THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
- Engineering and rapid selection of a low-affinity glucose/galactose-binding protein for a glucose biosensor.
- T. J. Amiss, D. B. Sherman, C. M. Nycz, S. A. Andaluz, and J. B. Pitner (2007)
Protein Sci.
16, 2350-2359
| Abstract »
| Full Text »
| PDF »
- Conformational changes of glucose/galactose-binding protein illuminated by open, unliganded, and ultra-high-resolution ligand-bound structures.
- M. J. Borrok, L. L. Kiessling, and K. T. Forest (2007)
Protein Sci.
16, 1032-1041
| Abstract »
| Full Text »
| PDF »
- Binding of Glucose to the D-Galactose/D-Glucose-Binding Protein from Escherichia coli Restores the Native Protein Secondary Structure and Thermostability That Are Lost upon Calcium Depletion.
- S. D'Auria, A. Ausili, A. Marabotti, A. Varriale, V. Scognamiglio, M. Staiano, E. Bertoli, M. Rossi, and F. Tanfani (2006)
J. Biochem.
139, 213-221
| Abstract »
| Full Text »
| PDF »
- Change in Rigidity in the Activated Form of the Glucose/Galactose Receptor from Escherichia coli: A Phenomenon that Will Be Key to the Development of Biosensors.
- I. Sokolov, V. Subba-Rao, and L. A. Luck (2006)
Biophys. J.
90, 1055-1063
| Abstract »
| Full Text »
| PDF »
- Computational prediction of native protein ligand-binding and enzyme active site sequences.
- R. Chakrabarti, A. M. Klibanov, and R. A. Friesner (2005)
PNAS
102, 10153-10158
| Abstract »
| Full Text »
| PDF »
- The Structure of a Cyanobacterial Sucrose-Phosphatase Reveals the Sugar Tongs That Release Free Sucrose in the Cell.
- S. Fieulaine, J. E. Lunn, F. Borel, and J.-L. Ferrer (2005)
PLANT CELL
17, 2049-2058
| Abstract »
| Full Text »
| PDF »
- Environmental pH Sensing: Resolving the VirA/VirG Two-Component System Inputs for Agrobacterium Pathogenesis.
- R. Gao and D. G. Lynn (2005)
J. Bacteriol.
187, 2182-2189
| Abstract »
| Full Text »
| PDF »
- Helix Induction in Antimicrobial Peptides by Alginate in Biofilms.
- C. Chan, L. L. Burrows, and C. M. Deber (2004)
J. Biol. Chem.
279, 38749-38754
| Abstract »
| Full Text »
| PDF »
- Computational design of receptors for an organophosphate surrogate of the nerve agent soman.
- M. Allert, S. S. Rizk, L. L. Looger, and H. W. Hellinga (2004)
PNAS
101, 7907-7912
| Abstract »
| Full Text »
| PDF »
- The Tp38 (TpMglB-2) Lipoprotein Binds Glucose in a Manner Consistent with Receptor Function in Treponema pallidum.
- R. K. Deka, M. S. Goldberg, K. E. Hagman, and M. V. Norgard (2004)
J. Bacteriol.
186, 2303-2308
| Abstract »
| Full Text »
| PDF »
- Exploiting luminescence spectroscopy to elucidate the interaction between sugar and a tryptophan residue in the lactose permease of Escherichia coli.
- J. L. Vazquez-Ibar, L. Guan, M. Svrakic, and H. R. Kaback (2003)
PNAS
100, 12706-12711
| Abstract »
| Full Text »
| PDF »
- In Vivo Imaging of the Dynamics of Glucose Uptake in the Cytosol of COS-7 Cells by Fluorescent Nanosensors.
- M. Fehr, S. Lalonde, I. Lager, M. W. Wolff, and W. B. Frommer (2003)
J. Biol. Chem.
278, 19127-19133
| Abstract »
| Full Text »
| PDF »
- Parallel Evolution of Ligand Specificity Between LacI/GalR Family Repressors and Periplasmic Sugar-Binding Proteins.
- K. Fukami-Kobayashi, Y. Tateno, and K. Nishikawa (2003)
Mol. Biol. Evol.
20, 267-277
| Abstract »
| Full Text »
| PDF »
- Cytoplasmic Loop Connecting Helices IV and V of the Melibiose Permease from Escherichia coli Is Involved in the Process of Na+-coupled Sugar Translocation.
- M. A. Dayem, C. Basquin, T. Pourcher, E. Cordat, and G. Leblanc (2003)
J. Biol. Chem.
278, 1518-1524
| Abstract »
| Full Text »
| PDF »
- Construction of a fluorescent biosensor family.
- R. M. De Lorimier, J. J. Smith, M. A. Dwyer, L. L. Looger, K. M. Sali, C. D. Paavola, S. S. Rizk, S. Sadigov, D. W. Conrad, L. Loew, et al. (2002)
Protein Sci.
11, 2655-2675
| Abstract »
| Full Text »
| PDF »
- From the Cover: Visualization of maltose uptake in living yeast cells by fluorescent nanosensors.
- M. Fehr, W. B. Frommer, and S. Lalonde (2002)
PNAS
99, 9846-9851
| Abstract »
| Full Text »
| PDF »
- Structural Basis for Broad Substrate Specificity in Higher Plant {beta}-D-Glucan Glucohydrolases.
- M. Hrmova, R. De Gori, B. J. Smith, J. K. Fairweather, H. Driguez, J. N. Varghese, and G. B. Fincher (2002)
PLANT CELL
14, 1033-1052
| Abstract »
| Full Text »
| PDF »
- Hinge-bending Motion of D-Allose-binding Protein from Escherichia coli. THREE OPEN CONFORMATIONS.
- U. Magnusson, B. N. Chaudhuri, J. Ko, C. Park, T. A. Jones, and S. L. Mowbray (2002)
J. Biol. Chem.
277, 14077-14084
| Abstract »
| Full Text »
| PDF »
- Design of Bioelectronic Interfaces by Exploiting Hinge-Bending Motions in Proteins.
- D. E. Benson, D. W. Conrad, R. M. de Lorimier, S. A. Trammell, and H. W. Hellinga (2001)
Science
293, 1641-1644
| Abstract »
| Full Text »
| PDF »
- Plasticity of quaternary structure: Twenty-two ways to form a LacI dimer.
- L. Swint-Kruse, C. R. Elam, J. W. Lin, D. R. Wycuff, and K. S. Matthews (2001)
Protein Sci.
10, 262-276
| Abstract »
| Full Text »
- Analysis of binding of the family 2a carbohydrate-binding module from Cellulomonas fimi xylanase 10A to cellulose: specificity and identification of functionally important amino acid residues.
- B. W. McLean, M. R. Bray, A. B. Boraston, N. R. Gilkes, C. A. Haynes, and D. G. Kilburn (2000)
Protein Eng. Des. Sel.
13, 801-809
| Abstract »
| Full Text »
| PDF »
- Cloning and DNA Sequence Analysis of an Immunogenic Glucose-Galactose MglB Lipoprotein Homologue from Brachyspira pilosicoli, the Agent of Colonic Spirochetosis.
- P. Zhang, X. Cheng, and G. E. Duhamel (2000)
Infect. Immun.
68, 4559-4565
| Abstract »
| Full Text »
| PDF »
- Substrate Recognition at the Cytoplasmic and Extracellular Binding Site of the Lactose Transport Protein of Streptococcus thermophilus.
- L. M. Veenhoff and B. Poolman (1999)
J. Biol. Chem.
274, 33244-33250
| Abstract »
| Full Text »
| PDF »
- Disulfide Bonding and Cysteine Accessibility in the alpha -Amino-3-hydroxy-5-methylisoxazole-4-propionic Acid Receptor Subunit GluRD. IMPLICATIONS FOR REDOX MODULATION OF GLUTAMATE RECEPTORS.
- R. Abele, M. Lampinen, K. Keinanen, and D. R. Madden (1998)
J. Biol. Chem.
273, 25132-25138
| Abstract »
| Full Text »
| PDF »
- Crystal Structure and Mutational Analysis of the Escherichia coli Putrescine Receptor. STRUCTURAL BASIS FOR SUBSTRATE SPECIFICITY.
- D. G. Vassylyev, H. Tomitori, K. Kashiwagi, K. Morikawa, and K. Igarashi (1998)
J. Biol. Chem.
273, 17604-17609
| Abstract »
| Full Text »
| PDF »
- Alteration of Substrate Affinities and Specificities of the Chlorella Hexose/H+ Symporters by Mutations and Construction of Chimeras.
- A. Will, R. Grassl, J. Erdmenger, T. Caspari, and W. Tanner (1998)
J. Biol. Chem.
273, 11456-11462
| Abstract »
| Full Text »
| PDF »
- Expression of a Soybean Hydroxyproline-Rich Glycoprotein Gene Is Correlated with Maturation of Roots.
- J. Hoon Ahn, Y. Choi, S.-G. Kim, Y. Myung Kwon, Y. Do Choi, and J. Seob Lee (1998)
Plant Physiology
116, 671-679
| Abstract »
| Full Text »
| PDF »
- Carbohydrate Starvation Stimulates Differential Expression of Rice alpha -Amylase Genes That Is Modulated through Complicated Transcriptional and Posttranscriptional Processes.
- J.-J. Sheu, T.-S. Yu, W.-F. Tong, and S.-M. Yu (1996)
J. Biol. Chem.
271, 26998-27004
| Abstract »
| Full Text »
| PDF »
- Crystal Structure of PotD, the Primary Receptor of the Polyamine Transport System in Escherichia coli.
- S. Sugiyama, D. G. Vassylyev, M. Matsushima, K. Kashiwagi, K. Igarashi, and K. Morikawa (1996)
J. Biol. Chem.
271, 9519-9525
| Abstract »
| Full Text »
| PDF »
- Secondary and tertiary structural effects on protein NMR chemical shifts: an ab initio approach.
- A. de Dios, J. Pearson, and E Oldfield (1993)
Science
260, 1491-1496
| Abstract »
| PDF »
- Atomic structure of adenosine deaminase complexed with a transition-state analog: understanding catalysis and immunodeficiency mutations.
- D. Wilson, F. Rudolph, and F. Quiocho (1991)
Science
252, 1278-1284
| Abstract »
| PDF »
- Predicting ligand-binding function in families of bacterial receptors.
- J. M. Johnson and G. M. Church (2000)
PNAS
97, 3965-3970
| Abstract »
| Full Text »
| PDF »
|
|
