1gax
From Proteopedia
(New page: 200px<br /> <applet load="1gax" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gax, resolution 2.9Å" /> '''CRYSTAL STRUCTURE OF...) |
|||
Line 1: | Line 1: | ||
- | [[Image:1gax.gif|left|200px]]<br /> | + | [[Image:1gax.gif|left|200px]]<br /><applet load="1gax" size="350" color="white" frame="true" align="right" spinBox="true" |
- | <applet load="1gax" size=" | + | |
caption="1gax, resolution 2.9Å" /> | caption="1gax, resolution 2.9Å" /> | ||
'''CRYSTAL STRUCTURE OF THERMUS THERMOPHILUS VALYL-TRNA SYNTHETASE COMPLEXED WITH TRNA(VAL) AND VALYL-ADENYLATE ANALOGUE'''<br /> | '''CRYSTAL STRUCTURE OF THERMUS THERMOPHILUS VALYL-TRNA SYNTHETASE COMPLEXED WITH TRNA(VAL) AND VALYL-ADENYLATE ANALOGUE'''<br /> | ||
==Overview== | ==Overview== | ||
- | Valyl-tRNA synthetase (ValRS) strictly discriminates the cognate L-valine | + | Valyl-tRNA synthetase (ValRS) strictly discriminates the cognate L-valine from the larger L-isoleucine and the isosteric L-threonine by the tRNA-dependent "double sieve" mechanism. In this study, we determined the 2.9 A crystal structure of a complex of Thermus thermophilus ValRS, tRNA(Val), and an analog of the Val-adenylate intermediate. The analog is bound in a pocket, where Pro(41) allows accommodation of the Val and Thr moieties but precludes the Ile moiety (the first sieve), on the aminoacylation domain. The editing domain, which hydrolyzes incorrectly synthesized Thr-tRNA(Val), is bound to the 3' adenosine of tRNA(Val). A contiguous pocket was found to accommodate the Thr moiety, but not the Val moiety (the second sieve). Furthermore, another Thr binding pocket for Thr-adenylate hydrolysis was suggested on the editing domain. |
==About this Structure== | ==About this Structure== | ||
- | 1GAX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with ZN and VAA as [http://en.wikipedia.org/wiki/ligands ligands]. The following page contains interesting information on the relation of 1GAX with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb16_1.html Aminoacyl-tRNA Synthetases]]. Active as [http://en.wikipedia.org/wiki/Valine--tRNA_ligase Valine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.9 6.1.1.9] Full crystallographic information is available from [http:// | + | 1GAX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=VAA:'>VAA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. The following page contains interesting information on the relation of 1GAX with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb16_1.html Aminoacyl-tRNA Synthetases]]. Active as [http://en.wikipedia.org/wiki/Valine--tRNA_ligase Valine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.9 6.1.1.9] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GAX OCA]. |
==Reference== | ==Reference== | ||
Line 18: | Line 17: | ||
[[Category: Fukai, S.]] | [[Category: Fukai, S.]] | ||
[[Category: Nureki, O.]] | [[Category: Nureki, O.]] | ||
- | [[Category: RSGI, RIKEN | + | [[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]] |
[[Category: Sekine, S.]] | [[Category: Sekine, S.]] | ||
[[Category: Shimada, A.]] | [[Category: Shimada, A.]] | ||
[[Category: Tao, J.]] | [[Category: Tao, J.]] | ||
- | [[Category: Vassylyev, D | + | [[Category: Vassylyev, D G.]] |
[[Category: Yokoyama, S.]] | [[Category: Yokoyama, S.]] | ||
[[Category: VAA]] | [[Category: VAA]] | ||
Line 34: | Line 33: | ||
[[Category: trna]] | [[Category: trna]] | ||
- | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:48:13 2008'' |
Revision as of 10:48, 21 February 2008
|
CRYSTAL STRUCTURE OF THERMUS THERMOPHILUS VALYL-TRNA SYNTHETASE COMPLEXED WITH TRNA(VAL) AND VALYL-ADENYLATE ANALOGUE
Overview
Valyl-tRNA synthetase (ValRS) strictly discriminates the cognate L-valine from the larger L-isoleucine and the isosteric L-threonine by the tRNA-dependent "double sieve" mechanism. In this study, we determined the 2.9 A crystal structure of a complex of Thermus thermophilus ValRS, tRNA(Val), and an analog of the Val-adenylate intermediate. The analog is bound in a pocket, where Pro(41) allows accommodation of the Val and Thr moieties but precludes the Ile moiety (the first sieve), on the aminoacylation domain. The editing domain, which hydrolyzes incorrectly synthesized Thr-tRNA(Val), is bound to the 3' adenosine of tRNA(Val). A contiguous pocket was found to accommodate the Thr moiety, but not the Val moiety (the second sieve). Furthermore, another Thr binding pocket for Thr-adenylate hydrolysis was suggested on the editing domain.
About this Structure
1GAX is a Single protein structure of sequence from Thermus thermophilus with and as ligands. The following page contains interesting information on the relation of 1GAX with [Aminoacyl-tRNA Synthetases]. Active as Valine--tRNA ligase, with EC number 6.1.1.9 Full crystallographic information is available from OCA.
Reference
Structural basis for double-sieve discrimination of L-valine from L-isoleucine and L-threonine by the complex of tRNA(Val) and valyl-tRNA synthetase., Fukai S, Nureki O, Sekine S, Shimada A, Tao J, Vassylyev DG, Yokoyama S, Cell. 2000 Nov 22;103(5):793-803. PMID:11114335
Page seeded by OCA on Thu Feb 21 12:48:13 2008
Categories: Aminoacyl-tRNA Synthetases | Single protein | Thermus thermophilus | Valine--tRNA ligase | Fukai, S. | Nureki, O. | RSGI, RIKEN Structural Genomics/Proteomics Initiative. | Sekine, S. | Shimada, A. | Tao, J. | Vassylyev, D G. | Yokoyama, S. | VAA | ZN | Coiled coil | Protein-rna complex | Riken structural genomics/proteomics initiative | Rossmann fold | Rsgi | Structural genomics | Trna