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 4 October 1985:
Vol. 230. no. 4721, pp. 32 - 36
DOI: 10.1126/science.3898365
Prev | Table of Contents | Next

Articles

Science, Vol 230, Issue 4721, 32-36
Copyright © 1985 by American Association for the Advancement of Science

articles

Structure of the GDP domain of EF-Tu and location of the amino acids homologous to ras oncogene proteins

F Jurnak

A 2.7 angstrom resolution x-ray diffraction analysis of a trypsin-modified form of the Escherichia coli elongation factor Tu reveals that the GDP-binding domain has a structure similar to that of other nucleotide-binding proteins. The GDP ligand is located at the COOH-terminal end of the beta sheet and is linked to the protein via a Mg2+ ion salt bridge. The location of the guanine ring is unusual; the purine ring is located on the outer edge of the domain, not deep within a hydrophobic pocket. The amino acids from Pro10 to Arg44 and from Gly59 to Glu190 have been assigned to the electron density with computer graphic techniques, and the resulting model is consistent with all known biochemical data. An analysis of the structure reveals that four regions of the amino acid sequence that are homologous with the family of ras oncogene proteins, termed p21, are located in the vicinity of the GDP-binding site, and most of the invariant amino acids shared by the proteins interact directly with the GDP ligand.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Effector Proteins Exert an Important Influence on the Signaling-active State of the Small GTPase Cdc42.
M. J. Phillips, G. Calero, B. Chan, S. Ramachandran, and R. A. Cerione (2008)
J. Biol. Chem. 283, 14153-14164
   Abstract »    Full Text »    PDF »
A Switch 3 Point Mutation in the {alpha} Subunit of Transducin Yields a Unique Dominant-negative Inhibitor.
R. Pereira and R. A. Cerione (2005)
J. Biol. Chem. 280, 35696-35703
   Abstract »    Full Text »    PDF »
Molecular Determinants for Cyclic Nucleotide Binding to the Regulatory Domains of Phosphodiesterase 2A.
A. Y. Wu, X.-B. Tang, S. E. Martinez, K. Ikeda, and J. A. Beavo (2004)
J. Biol. Chem. 279, 37928-37938
   Abstract »    Full Text »    PDF »
Induced nucleotide specificity in a GTPase.
S.-o. Shan and P. Walter (2003)
PNAS 100, 4480-4485
   Abstract »    Full Text »    PDF »
Escherichia coli DNA Polymerase III tau - and gamma -Subunit Conserved Residues Required for Activity In Vivo and In Vitro.
J. R. Walker, C. Hervas, J. D. Ross, A. Blinkova, M. J. Walbridge, E. J. Pumarega, M.-O. Park, and H. R. Neely (2000)
J. Bacteriol. 182, 6106-6113
   Abstract »    Full Text »
Crystal structure of ERA: A GTPase-dependent cell cycle regulator containing an RNA binding motif.
X. Chen, D. L. Court, and X. Ji (1999)
PNAS 96, 8396-8401
   Abstract »    Full Text »    PDF »
Sequence of Events Underlying the Allosteric Transition of Rod Cyclic Nucleotide-gated Channels.
E. R. Sunderman and W. N. Zagotta (1999)
J. Gen. Physiol. 113, 621-640
   Abstract »    Full Text »    PDF »
EPR Spectroscopy of VO2+-ATP Bound to Catalytic Site 3 of Chloroplast F1-ATPase from Chlamydomonas Reveals Changes in Metal Ligation Resulting from Mutations to the Phosphate-binding Loop Threonine (beta T168).
W. Chen, R. LoBrutto, and W. D. Frasch (1999)
J. Biol. Chem. 274, 7089-7094
   Abstract »    Full Text »    PDF »
In Vitro Study of Two Dominant Inhibitory GTPase Mutants of Escherichia coli Translation Initiation Factor IF2. DIRECT EVIDENCE THAT GTP HYDROLYSIS IS NECESSARY FOR FACTOR RECYCLING.
S. Luchin, H. Putzer, J. W. B. Hershey, Y. Cenatiempo, M. Grunberg-Manago, and S. Laalami (1999)
J. Biol. Chem. 274, 6074-6079
   Abstract »    Full Text »    PDF »
Roles of Residues in Mammalian Mitochondrial Elongation Factor Ts in the Interaction with Mitochondrial and Bacterial Elongation Factor Tu.
Y. Zhang and L. L. Spremulli (1998)
J. Biol. Chem. 273, 28142-28148
   Abstract »    Full Text »    PDF »
MgADP Antagonism to Mg2+-independent ATP Binding of the Sulfonylurea Receptor SUR1.
K. Ueda, N. Inagaki, and S. Seino (1997)
J. Biol. Chem. 272, 22983-22986
   Abstract »    Full Text »    PDF »
Complementation of sporulation and motility defects in a prokaryote by a eukaryotic GTPase.
P. L. Hartzell (1997)
PNAS 94, 9881-9886
   Abstract »    Full Text »    PDF »
Communication between Switch II and Switch III of the Transducin alpha  Subunit Is Essential for Target Activation.
Q. Li and R. A. Cerione (1997)
J. Biol. Chem. 272, 21673-21676
   Abstract »    Full Text »    PDF »
Point Mutations in Human {beta} Cardiac Myosin Heavy Chain Have Differential Effects on Sarcomeric Structure and Assembly: An ATP Binding Site Change Disrupts Both Thick and Thin Filaments, Whereas Hypertrophic Cardiomyopathy Mutations Display Normal Assembly.
K. D. Becker, K. R. Gottshall, R. Hickey, J.-C. Perriard, and K. R. Chien (1997)
J. Cell Biol. 137, 131-140
   Abstract »    Full Text »    PDF »
Biochemical Analyses of Mutations in the HSV-1 Helicase-Primase That Alter ATP Hydrolysis, DNA Unwinding, and Coupling Between Hydrolysis and Unwinding.
K. L. Graves-Woodward, J. Gottlieb, M. D. Challberg, and S. K. Weller (1997)
J. Biol. Chem. 272, 4623-4630
   Abstract »    Full Text »    PDF »
Synthesis and Effect of Nonhydrolyzable Xanthosine Triphosphate Derivatives on Prenylation of Rab5D136N.
I. Yanachkov, J. Y. Pan, M. Wessling-Resnick, and G. E. Wright (1997)
Mol. Pharmacol. 51, 47-51
   Abstract »    Full Text »
The alpha 3beta 3gamma Subcomplex of the F1-ATPase from the Thermophilic Bacillus PS3 with the beta T165S Substitution Does Not Entrap Inhibitory MgADP in a Catalytic Site during Turnover.
J.-M. Jault, C. Dou, N. B. Grodsky, T. Matsui, M. Yoshida, and W. S. Allison (1996)
J. Biol. Chem. 271, 28818-28824
   Abstract »    Full Text »    PDF »
Identification of Key Amino Acids in a Conserved cGMP-binding Site of cGMP-binding Phosphodiesterases. A PUTATIVE NKXnD MOTIF FOR cGMP BINDING.
I. V. Turko, T. L. Haik, L. M. McAllister-Lucas, F. Burns, S. H. Francis, and J. D. Corbin (1996)
J. Biol. Chem. 271, 22240-22244
   Abstract »    Full Text »    PDF »
Domains of DnaA Protein Involved in Interaction with DnaB Protein, and in Unwinding the Escherichia coli Chromosomal Origin.
J. Marszalek, W. Zhang, T. R. Hupp, C. Margulies, K. M. Carr, S. Cherry, and J. M. Kaguni (1996)
J. Biol. Chem. 271, 18535-18542
   Abstract »    Full Text »    PDF »
Intragenic Suppressors of P-loop Mutations in the beta-Subunit of the Mitochondrial ATPase in the Yeast Saccharomyces cerevisiae.
H. Shen, A. Sosa-Peinado, and D. M. Mueller (1996)
J. Biol. Chem. 271, 11844-11851
   Abstract »    Full Text »    PDF »
The DNA Binding Site(s) of the Escherichia coli RecA Protein.
W. M. Rehrauer and S. C. Kowalczykowski (1996)
J. Biol. Chem. 271, 11996-12002
   Abstract »    Full Text »    PDF »
Inactivation of Chloramphenicol by O-Phosphorylation.
R. H. Mosher, D. J. Camp, K. Yang, M. P. Brown, W. V. Shaw, and L. C. Vining (1995)
J. Biol. Chem. 270, 27000-27006
   Abstract »    Full Text »    PDF »
Unexpected Structural Requirements for GTPase Activity of the Interferon-induced MxA Protein.
M. Schwemmle, M. F. Richter, C. Herrmann, N. Nassar, and P. Staeheli (1995)
J. Biol. Chem. 270, 13518-13523
   Abstract »    Full Text »    PDF »
Switching Nucleotide Specificity of Ha-Ras p21 by a Single Amino Acid Substitution at Aspartate 119.
J.-M. Zhong, M.-C. Chen-Hwang, and Y.-W. Hwang (1995)
J. Biol. Chem. 270, 10002-10007
   Abstract »    Full Text »    PDF »
Separate GTP binding and GTPase activating domains of a G alpha subunit.
D. Markby, R Onrust, and H. Bourne (1993)
Science 262, 1895-1901
   Abstract »    PDF »
GTP hydrolysis in protein synthesis: two for Tu?.
P Schimmel (1993)
Science 259, 1264-1265
   PDF »
Toward a model for the interaction between elongation factor Tu and the ribosome.
A Weijland and A Parmeggiani (1993)
Science 259, 1311-1314
   Abstract »    PDF »
A mRNA localized to the vegetal cortex of Xenopus oocytes encodes a protein with a nanos-like zinc finger domain.
L. Mosquera, C. Forristall, Y. Zhou, and M. L. King (1993)
Development 117, 377-386
   Abstract »    PDF »
Evidence that eukaryotes and eocyte prokaryotes are immediate relatives.
M. Rivera and J. Lake (1992)
Science 257, 74-76
   Abstract »    PDF »
A bacterial system for investigating transport effects of cystic fibrosis--associated mutations.
A. Gibson, L. Wagner, F. Collins, and D. Oxender (1991)
Science 254, 109-111
   Abstract »    PDF »
Structure of ras proteins.
L Tong, M. Milburn, A. de Vos, and S. Kim (1989)
Science 245, 244
   PDF »
Three-dimensional structure of an oncogene protein: catalytic domain of human c-H-ras p21.
A. de Vos, L Tong, M. Milburn, P. Matias, J Jancarik, S Noguchi, S Nishimura, K Miura, E Ohtsuka, and S. Kim (1988)
Science 239, 888-893
   Abstract »    PDF »
cAMP-dependent Protein Kinase: A Framework for a Diverse Family of Enzymes.
S.S. Taylor, J.A. Buechler, L.W. Slice, D.K. Knighton, S. Durgerian, G.E. Ringheim, J.J. Neitzel, W.M. Yonemoto, J.M. Sowadski, and W. Dospmann (1988)
Cold Spring Harb Symp Quant Biol 53, 121-130
   Abstract »    PDF »
Structures of the Genes Coding for G-protein a Subunits from Mammalian and Yeast Cells.
Y. Kaziro, H. Itoh, T. Kozasa, R. Toyama, T. Tsukamoto, M. Matsuoka, M. Nakafuku, T. Obara, T. Takagi, and R. Hernandez (1988)
Cold Spring Harb Symp Quant Biol 53, 209-220
   Abstract »    PDF »
Mutations Probe Structure and Function of G-protein {alpha} Chains.
H.R. Bourne, S.B. Masters, R.T. Miller, K.A. Sullivan, and W. Heideman (1988)
Cold Spring Harb Symp Quant Biol 53, 221-228
   Abstract »    PDF »
Functions of G-protein Subunits.
E.J. Neer, S.-Y. Kim, S.-L. Ang, D.B. Bloch, K.D. Bloch, Y. Kawahara, C. Tolman, R. Lee, D. Logothetis, D. Kim, et al. (1988)
Cold Spring Harb Symp Quant Biol 53, 241-246
   Abstract »    PDF »
ras Oncogene Proteins: Three-dimensional Structures, Functional Implications, and a Model for Signal Transducer.
S.-H. Kim, A.M. de Vos, L. Tong, M.V. Milburn, P.M. Matias, J. Jancarik, E. Ohtsuka, and S. Nishimura (1988)
Cold Spring Harb Symp Quant Biol 53, 273-281
   Abstract »    PDF »
Regulation of Vesicular Traffic by a GTP-binding Protein on the Cytoplasmic Surface of Secretory Vesicles in Yeast.
P. J. Novick, B. Goud, A. Salminen, N.C. Walworth, J. Nair, and M. Potenza (1988)
Cold Spring Harb Symp Quant Biol 53, 637-647
   Abstract »    PDF »
Structure/Function Studies of the ras Protein.
I.S. Sigal, M.S. Marshall, M.D. Schaber, U.S. Vogel, E.M. Scolnick, and J.B. Gibbs (1988)
Cold Spring Harb Symp Quant Biol 53, 863-869
   Abstract »    PDF »
A cytoplasmic protein stimulates normal N-ras p21 GTPase, but does not affect oncogenic mutants.
M Trahey and F McCormick (1987)
Science 238, 542-545
   Abstract »    PDF »
Promotion of tubulin assembly by aluminum ion in vitro.
T. Macdonald, W. Humphreys, and R. Martin (1987)
Science 236, 183-186
   Abstract »    PDF »
Identification of specific transducin alpha subunits in retinal rod and cone photoreceptors.
C. Lerea, D. Somers, J. Hurley, I. Klock, and A. Bunt-Milam (1986)
Science 234, 77-80
   Abstract »    PDF »
The oncogenic activation of human p21ras by a novel mechanism.
M Walter, S. Clark, and A. Levinson (1986)
Science 233, 649-652
   Abstract »    PDF »


To Advertise     Find Products

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