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 11 March 1994:
Vol. 263. no. 5152, pp. 1432 - 1436
DOI: 10.1126/science.8128224
Prev | Table of Contents | Next

Articles

Science, Vol 263, Issue 5152, 1432-1436
Copyright © 1994 by American Association for the Advancement of Science

articles

Crystal structures at 2.5 angstrom resolution of seryl-tRNA synthetase complexed with two analogs of seryl adenylate

H Belrhali, A Yaremchuk, M Tukalo, K Larsen, C Berthet-Colominas, R Leberman, B Beijer, B Sproat, J Als-Nielsen, G Grubel, and al. et

EMBL Grenoble Outstation, France.

Crystal structures of seryl-tRNA synthetase from Thermus thermophilus complexed with two different analogs of seryl adenylate have been determined at 2.5 A resolution. The first complex is between the enzyme and seryl-hydroxamate-AMP (adenosine monophosphate), produced enzymatically in the crystal from adenosine triphosphate (ATP) and serine hydroxamate, and the second is with a synthetic analog of seryl adenylate (5'-O-[N-(L-seryl)-sulfamoyl]adenosine), which is a strong inhibitor of the enzyme. Both molecules are bound in a similar fashion by a network of hydrogen bond interactions in a deep hydrophilic cleft formed by the antiparallel beta sheet and surrounding loops of the synthetase catalytic domain. Four regions in the primary sequence are involved in the interactions, including the motif 2 and 3 regions of class 2 synthetases. Apart from the specific recognition of the serine side chain, the interactions are likely to be similar in all class 2 synthetases.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Two Crystal Structures of Lysyl-tRNA Synthetase from Bacillus stearothermophilus in Complex with Lysyladenylate-Like Compounds: Insights into the Irreversible Formation of the Enzyme-Bound Adenylate of L-Lysine Hydroxamate.
H. Sakurama, T. Takita, B. Mikami, T. Itoh, K. Yasukawa, and K. Inouye (2009)
J. Biochem. 145, 555-563
   Abstract »    Full Text »    PDF »
Participation of the Lys313-Ile333 Sequence of the Purinergic P2X4 Receptor in Agonist Binding and Transduction of Signals to the Channel Gate.
Z. Yan, Z. Liang, T. Obsil, and S. S. Stojilkovic (2006)
J. Biol. Chem. 281, 32649-32659
   Abstract »    Full Text »    PDF »
Fidelity of seryl-tRNA synthetase to binding of natural amino acids from HierDock first principles computations.
C. L. McClendon, N. Vaidehi, V. W. T. Kam, D. Zhang, and W. A. Goddard III (2006)
Protein Eng. Des. Sel. 19, 195-203
   Abstract »    Full Text »    PDF »
Molecular Determinants of the Agonist Binding Domain of a P2X Receptor Channel.
Z. Yan, Z. Liang, M. Tomic, T. Obsil, and S. S. Stojilkovic (2005)
Mol. Pharmacol. 67, 1078-1088
   Abstract »    Full Text »    PDF »
Breaking sieve for steric exclusion of a noncognate amino acid from active site of a tRNA synthetase.
M. A. Swairjo and P. R. Schimmel (2005)
PNAS 102, 988-993
   Abstract »    Full Text »    PDF »
Dual Mode Recognition of Two Isoacceptor tRNAs by Mammalian Mitochondrial Seryl-tRNA Synthetase.
N. Shimada, T. Suzuki, and K. Watanabe (2001)
J. Biol. Chem. 276, 46770-46778
   Abstract »    Full Text »    PDF »
Proofreading and Aminoacylation of tRNAs Before Export from the Nucleus.
E. Lund and J. E. Dahlberg (1998)
Science 282, 2082-2085
   Abstract »    Full Text »
The first step of aminoacylation at the atomic level in histidyl-tRNA synthetase.
J. G. Arnez, J. G. Augustine, D. Moras, and C. S. Francklyn (1997)
PNAS 94, 7144-7149
   Abstract »    Full Text »    PDF »
Defining the Active Site of Yeast Seryl-tRNA Synthetase. MUTATIONS IN MOTIF 2LOOP RESIDUES AFFECT tRNA-DEPENDENT AMINO ACID RECOGNITION.
B. Lenhard, B. Lenhard, I. Landeka, and D. Soll (1997)
J. Biol. Chem. 272, 1136-1141
   Abstract »    Full Text »    PDF »
Expression of Rat Aspartyl-tRNA Synthetase in Saccharomyces cerevisiae. ROLE OF THE NH2-TERMINAL POLYPEPTIDE EXTENSION ON ENZYME ACTIVITY AND STABILITY.
F. Agou, J.-P. Waller, and M. Mirande (1996)
J. Biol. Chem. 271, 29295-29303
   Abstract »    Full Text »    PDF »
Essential Amino Acids Regulate Fatty Acid Synthase Expression through an Uncharged Transfer RNA-dependent Mechanism.
S. M. Dudek and C. F. Semenkovich (1995)
J. Biol. Chem. 270, 29323-29329
   Abstract »    Full Text »    PDF »
Aminoacyl-RNA synthesis catalyzed by an RNA.
M Illangasekare, G Sanchez, T Nickles, and M Yarus (1995)
Science 267, 643-647
   Abstract »    PDF »
The 2.9 A crystal structure of T. thermophilus seryl-tRNA synthetase complexed with tRNA(Ser).
V Biou, A Yaremchuk, M Tukalo, and S Cusack (1994)
Science 263, 1404-1410
   Abstract »    PDF »


To Advertise     Find Products

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