1gax: Difference between revisions
New page: left|200px<br /> <applet load="1gax" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gax, resolution 2.9Å" /> '''CRYSTAL STRUCTURE OF... |
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[[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" | ||
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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== | ||
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[[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]] | ||
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[[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 13:48, 21 February 2008
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CRYSTAL STRUCTURE OF THERMUS THERMOPHILUS VALYL-TRNA SYNTHETASE COMPLEXED WITH TRNA(VAL) AND VALYL-ADENYLATE ANALOGUE
OverviewOverview
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 StructureAbout 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.
ReferenceReference
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
Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Pages with broken file links
- 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