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 29 November 1991:
Vol. 254. no. 5036, pp. 1342 - 1347
DOI: 10.1126/science.1660187
Prev | Table of Contents | Next

Articles

Science, Vol 254, Issue 5036, 1342-1347
Copyright © 1991 by American Association for the Advancement of Science

articles

Three-dimensional structures of the ligand-binding domain of the bacterial aspartate receptor with and without a ligand

MV Milburn, GG Prive, DL Milligan, WG Scott, J Yeh, J Jancarik, DE Koshland Jr, and SH Kim

Department of Chemistry, University of California, Berkeley 94720.

The three-dimensional structure of an active, disulfide cross-linked dimer of the ligand-binding domain of the Salmonella typhimurium aspartate receptor and that of an aspartate complex have been determined by x-ray crystallographic methods at 2.4 and 2.0 angstrom (A) resolution, respectively. A single subunit is a four-alpha-helix bundle with two long amino-terminal and carboxyl-terminal helices and two shorter helices that form a cylinder 20 A in diameter and more than 70 A long. The two subunits in the disulfide-bonded dimer are related by a crystallographic twofold axis in the apo structure, but by a noncrystallographic twofold axis in the aspartate complex structure. The latter structure reveals that the ligand binding site is located more than 60 A from the presumed membrane surface and is at the interface of the two subunits. Aspartate binds between two alpha helices from one subunit and one alpha helix from the other in a highly charged pocket formed by three arginines. The comparison of the apo and aspartate complex structures shows only small structural changes in the individual subunits, except for one loop region that is disordered, but the subunits appear to change orientation relative to each other. The structures of the two forms of this protein provide a step toward understanding the mechanisms of transmembrane signaling.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Role of HAMP domains in chemotaxis signaling by bacterial chemoreceptors.
C. M. Khursigara, X. Wu, P. Zhang, J. Lefman, and S. Subramaniam (2008)
PNAS 105, 16555-16560
   Abstract »    Full Text »    PDF »
Stimulus Perception in Bacterial Signal-Transducing Histidine Kinases.
T. Mascher, J. D. Helmann, and G. Unden (2006)
Microbiol. Mol. Biol. Rev. 70, 910-938
   Abstract »    Full Text »    PDF »
Self-assembly of receptor/signaling complexes in bacterial chemotaxis.
P. M. Wolanin, M. D. Baker, N. R. Francis, D. R. Thomas, D. J. DeRosier, and J. B. Stock (2006)
PNAS 103, 14313-14318
   Abstract »    Full Text »    PDF »
Control of Chemotactic Signal Gain via Modulation of a Pre-formed Receptor Array.
H. Irieda, M. Homma, M. Homma, and I. Kawagishi (2006)
J. Biol. Chem. 281, 23880-23886
   Abstract »    Full Text »    PDF »
Differential Recognition of Citrate and a Metal-Citrate Complex by the Bacterial Chemoreceptor Tcp.
T. Iwama, Y. Ito, H. Aoki, H. Sakamoto, S. Yamagata, K. Kawai, and I. Kawagishi (2006)
J. Biol. Chem. 281, 17727-17735
   Abstract »    Full Text »    PDF »
Mutationally Altered Signal Output in the Nart (NarX-Tar) Hybrid Chemoreceptor.
S. M. Ward, A. F. Bormans, and M. D. Manson (2006)
J. Bacteriol. 188, 3944-3951
   Abstract »    Full Text »    PDF »
The Identification of a Minimal Dimerization Motif QXXS That Enables Homo- and Hetero-association of Transmembrane Helices in Vivo.
N. Sal-Man, D. Gerber, and Y. Shai (2005)
J. Biol. Chem. 280, 27449-27457
   Abstract »    Full Text »    PDF »
Hydrophobic interactions drive ligand-receptor recognition for activation and inhibition of staphylococcal quorum sensing.
J. S. Wright III, G. J. Lyon, E. A. George, T. W. Muir, and R. P. Novick (2004)
PNAS 101, 16168-16173
   Abstract »    Full Text »    PDF »
Ligand-Specific Activation of Escherichia coli Chemoreceptor Transmethylation.
F. M. Antommattei, J. B. Munzner, and R. M. Weis (2004)
J. Bacteriol. 186, 7556-7563
   Abstract »    Full Text »    PDF »
Negative Cooperativity of Glutamate Binding in the Dimeric Metabotropic Glutamate Receptor Subtype 1.
Y. Suzuki, E. Moriyoshi, D. Tsuchiya, and H. Jingami (2004)
J. Biol. Chem. 279, 35526-35534
   Abstract »    Full Text »    PDF »
Three-Dimensional Electron Microscopic Imaging of Membrane Invaginations in Escherichia coli Overproducing the Chemotaxis Receptor Tsr.
J. Lefman, P. Zhang, T. Hirai, R. M. Weis, J. Juliani, D. Bliss, M. Kessel, E. Bos, P. J. Peters, and S. Subramaniam (2004)
J. Bacteriol. 186, 5052-5061
   Abstract »    Full Text »    PDF »
CHEMOTAXIS-GUIDED MOVEMENTS IN BACTERIA.
R. Lux and W. Shi (2004)
Critical Reviews in Oral Biology & Medicine 15, 207-220
   Abstract »    Full Text »    PDF »
A Redox-controlled Molecular Switch Revealed by the Crystal Structure of a Bacterial Heme PAS Sensor.
H. Kurokawa, D.-S. Lee, M. Watanabe, I. Sagami, B. Mikami, C. S. Raman, and T. Shimizu (2004)
J. Biol. Chem. 279, 20186-20193
   Abstract »    Full Text »    PDF »
Evidence of an Intramolecular Interaction between the Two Domains of the BlaR1 Penicillin Receptor during the Signal Transduction.
S. Hanique, M.-L. Colombo, E. Goormaghtigh, P. Soumillion, J.-M. Frere, and B. Joris (2004)
J. Biol. Chem. 279, 14264-14272
   Abstract »    Full Text »    PDF »
Attractant binding alters arrangement of chemoreceptor dimers within its cluster at a cell pole.
M. Homma, D. Shiomi, M. Homma, and I. Kawagishi (2004)
PNAS 101, 3462-3467
   Abstract »    Full Text »    PDF »
Crosslinking snapshots of bacterial chemoreceptor squads.
C. A. Studdert and J. S. Parkinson (2004)
PNAS 101, 2117-2122
   Abstract »    Full Text »    PDF »
The NMR Structure of the Sensory Domain of the Membranous Two-component Fumarate Sensor (Histidine Protein Kinase) DcuS of Escherichia coli.
L. Pappalardo, I. G. Janausch, V. Vijayan, E. Zientz, J. Junker, W. Peti, M. Zweckstetter, G. Unden, and C. Griesinger (2003)
J. Biol. Chem. 278, 39185-39188
   Abstract »    Full Text »    PDF »
The Structure of the Periplasmic Ligand-binding Domain of the Sensor Kinase CitA Reveals the First Extracellular PAS Domain.
S. Reinelt, E. Hofmann, T. Gerharz, M. Bott, and D. R. Madden (2003)
J. Biol. Chem. 278, 39189-39196
   Abstract »    Full Text »    PDF »
Electron Microscopic Analysis of Membrane Assemblies Formed by the Bacterial Chemotaxis Receptor Tsr.
R. M. Weis, T. Hirai, A. Chalah, M. Kessel, P. J. Peters, and S. Subramaniam (2003)
J. Bacteriol. 185, 3636-3643
   Abstract »    Full Text »    PDF »
Rotational On-off Switching of a Hybrid Membrane Sensor Kinase Tar-ArcB in Escherichia coli.
O. Kwon, D. Georgellis, and E. C. C. Lin (2003)
J. Biol. Chem. 278, 13192-13195
   Abstract »    Full Text »    PDF »
Common Extracellular Sensory Domains in Transmembrane Receptors for Diverse Signal Transduction Pathways in Bacteria and Archaea.
I. B. Zhulin, A. N. Nikolskaya, and M. Y. Galperin (2003)
J. Bacteriol. 185, 285-294
   Abstract »    Full Text »    PDF »
Conserved Amplification of Chemotactic Responses through Chemoreceptor Interactions.
A. C. Lamanna, J. E. Gestwicki, L. E. Strong, S. L. Borchardt, R. M. Owen, and L. L. Kiessling (2002)
J. Bacteriol. 184, 4981-4987
   Abstract »    Full Text »    PDF »
Dynamic and clustering model of bacterial chemotaxis receptors: Structural basis for signaling and high sensitivity.
S.-H. Kim, W. Wang, and K. K. Kim (2002)
PNAS 99, 11611-11615
   Abstract »    Full Text »    PDF »
Cooperativity between bacterial chemotaxis receptors.
J. J. Falke (2002)
PNAS 99, 6530-6532
   Full Text »    PDF »
Mechanism of Coupling of Transport to Hydrolysis in Bacterial ATP-Binding Cassette Transporters.
A. L. Davidson (2002)
J. Bacteriol. 184, 1225-1233
   Full Text »    PDF »
Bright Lights, Abundant Operons--Fluorescence and Genomic Technologies Advance Studies of Bacterial Locomotion and Signal Transduction: Review of the BLAST Meeting, Cuernavaca, Mexico, 14 to 19 January 2001.
R. B. Bourret, N. W. Charon, A. M. Stock, and A. H. West (2002)
J. Bacteriol. 184, 1-17
   Full Text »    PDF »
Evidence That Both Ligand Binding and Covalent Adaptation Drive a Two-State Equilibrium in the Aspartate Receptor Signaling Complex.
J. A. Bornhorst and J. J. Falke (2001)
J. Gen. Physiol. 118, 693-710
   Abstract »    Full Text »    PDF »
Complementing Yeast rho1 Mutation Groups with Distinct Functional Defects.
A. Saka, M. Abe, H. Okano, M. Minemura, H. Qadota, T. Utsugi, A. Mino, K. Tanaka, Y. Takai, and Y. Ohya (2001)
J. Biol. Chem. 276, 46165-46171
   Abstract »    Full Text »    PDF »
Rhodopsin: Structural Basis of Molecular Physiology.
S. T. Menon, M. Han, and T. P. Sakmar (2001)
Physiol Rev 81, 1659-1688
   Abstract »    Full Text »    PDF »
Substitutions in the Periplasmic Domain of Low-Abundance Chemoreceptor Trg That Induce or Reduce Transmembrane Signaling: Kinase Activation and Context Effects.
B. D. Beel and G. L. Hazelbauer (2001)
J. Bacteriol. 183, 671-679
   Abstract »    Full Text »    PDF »
Mutational Analysis of Ligand Recognition by Tcp, the Citrate Chemoreceptor of Salmonella enterica Serovar Typhimurium.
T. Iwama, K.-I. Nakao, H. Nakazato, S. Yamagata, M. Homma, and I. Kawagishi (2000)
J. Bacteriol. 182, 1437-1441
   Abstract »    Full Text »    PDF »
The Escherichia coli aspartate receptor: sequence specificity of a transmembrane helix studied by hydrophobic-biased random mutagenesis.
C. J. Jeffery and D. E. Koshland Jr (1999)
Protein Eng. Des. Sel. 12, 863-872
   Abstract »    Full Text »    PDF »
Folding funnels and binding mechanisms.
B. Ma, S. Kumar, C.-J. Tsai, and R. Nussinov (1999)
Protein Eng. Des. Sel. 12, 713-720
   Abstract »    Full Text »    PDF »
Model of maltose-binding protein/chemoreceptor complex supports intrasubunit signaling mechanism.
Y. Zhang, P. J. Gardina, A. S. Kuebler, H. S. Kang, J. A. Christopher, and M. D. Manson (1999)
PNAS 96, 939-944
   Abstract »    Full Text »    PDF »
Intersubunit Interaction between Transmembrane Helices of the Bacterial Aspartate Chemoreceptor Homodimer.
T. Umemura, I. Tatsuno, M. Shibasaki, M. Homma, and I. Kawagishi (1998)
J. Biol. Chem. 273, 30110-30115
   Abstract »    Full Text »    PDF »
Detection of a Conserved alpha -Helix in the Kinase-docking Region of the Aspartate Receptor by Cysteine and Disulfide Scanning.
R. B. Bass and J. J. Falke (1998)
J. Biol. Chem. 273, 25006-25014
   Abstract »    Full Text »    PDF »
Two-domain reconstitution of a functional protein histidine kinase.
H. Park, S. K. Saha, and M. Inouye (1998)
PNAS 95, 6728-6732
   Abstract »    Full Text »    PDF »
Water-soluble Nicotinic Acetylcholine Receptor Formed by alpha 7 Subunit Extracellular Domains.
G. B. Wells, R. Anand, F. Wang, and J. Lindstrom (1998)
J. Biol. Chem. 273, 964-973
   Abstract »    Full Text »    PDF »
Cysteine and Disulfide Scanning Reveals a Regulatory alpha -Helix in the Cytoplasmic Domain of the Aspartate Receptor.
M. A. Danielson, R. B. Bass, and J. J. Falke (1997)
J. Biol. Chem. 272, 32878-32888
   Abstract »    Full Text »    PDF »
Converting a transmembrane receptor to a soluble receptor: Recognition domain to effector domain signaling after excision of the transmembrane domain.
K. M. Ottemann and D. E. Koshland Jr. (1997)
PNAS 94, 11201-11204
   Abstract »    Full Text »    PDF »
Uncoupling of Ligand-binding Affinity of the Bacterial Serine Chemoreceptor from Methylation- and Temperature-modulated Signaling States.
T. Iwama, M. Homma, and I. Kawagishi (1997)
J. Biol. Chem. 272, 13810-13815
   Abstract »    Full Text »    PDF »
An Aspartate/Insulin Receptor Chimera Mitogenically Activates Fibroblasts.
H.-P. Biemann, S. L. Harmer, and D. E. Koshland Jr. (1996)
J. Biol. Chem. 271, 27927-27930
   Abstract »    Full Text »    PDF »
Signal Detection by the PhoQ Sensor-Transmitter. CHARACTERIZATION OF THE SENSOR DOMAIN AND A RESPONSE-IMPAIRED MUTANT THAT IDENTIFIES LIGAND-BINDING DETERMINANTS.
C. D. Waldburger and R. T. Sauer (1996)
J. Biol. Chem. 271, 26630-26636
   Abstract »    Full Text »    PDF »
Maltose-binding Protein Containing an Interdomain Disulfide Bridge Confers a Dominant-negative Phenotype for Transport and Chemotaxis.
Y. Zhang, D. E. Mannering, A. L. Davidson, N. Yao, and M. D. Manson (1996)
J. Biol. Chem. 271, 17881-17889
   Abstract »    Full Text »    PDF »
Role of alpha -Helical Coiled-coil Interactions in Receptor Dimerization, Signaling, and Adaptation during Bacterial Chemotaxis.
M. G. Surette and J. B. Stock (1996)
J. Biol. Chem. 271, 17966-17973
   Abstract »    Full Text »    PDF »
The N-terminal Cytoplasmic Tail of the Aspartate Receptor Is Not Essential in Signal Transduction of Bacterial Chemotaxis.
X. Chen and D. E. Koshland , Jr. (1995)
J. Biol. Chem. 270, 24038-24042
   Abstract »    Full Text »    PDF »
Lock On/Off Disulfides Identify the Transmembrane Signaling Helix of the Aspartate Receptor.
S. A. Chervitz and J. J. Falke (1995)
J. Biol. Chem. 270, 24043-24053
   Abstract »    Full Text »    PDF »
Polar location of the chemoreceptor complex in the Escherichia coli cell.
Maddock JR and L Shapiro (1993)
Science 259, 1717-1723
   Abstract »    PDF »
Receptors and Transmembrane Signaling.
B.L. Stoddard, H.-P. Biemann, and D.E. Koshland Jr. (1992)
Cold Spring Harb Symp Quant Biol 57, 1-15
   Abstract »    PDF »
A Model for Transmembrane Signaling in a Bacterial Chemotaxis Receptor.
S.-H. Kim, G.G. Prive, J. Yeh, W.G. Scott, and M.V. Milburn (1992)
Cold Spring Harb Symp Quant Biol 57, 17-24
   Abstract »    PDF »
Mutations That Affect Ligand Binding to the Escherichia coli Aspartate Receptor. IMPLICATIONS FOR TRANSMEMBRANE SIGNALING.
A. M. Bjorkman, P. Dunten, M. O. J. Sandgren, V. N. Dwarakanath, and S. L. Mowbray (2001)
J. Biol. Chem. 276, 2808-2815
   Abstract »    Full Text »    PDF »


To Advertise     Find Products

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