1gax

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|PDB= 1gax |SIZE=350|CAPTION= <scene name='initialview01'>1gax</scene>, resolution 2.9&Aring;
|PDB= 1gax |SIZE=350|CAPTION= <scene name='initialview01'>1gax</scene>, resolution 2.9&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=VAA:N-[VALINYL]-N'-[ADENOSYL]-DIAMINOSUFONE'>VAA</scene>
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|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=VAA:N-[VALINYL]-N&#39;-[ADENOSYL]-DIAMINOSUFONE'>VAA</scene>
|ACTIVITY= [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]
|ACTIVITY= [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]
|GENE=
|GENE=
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[[Category: trna]]
[[Category: trna]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:20:40 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 11:54:35 2008''

Revision as of 09:54, 23 March 2008

Image:1gax.gif


PDB ID 1gax

Drag the structure with the mouse to rotate
, resolution 2.9Å
Ligands: and
Activity: Valine--tRNA ligase, with EC number 6.1.1.9
Coordinates: save as pdb, mmCIF, xml



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. The following page contains interesting information on the relation of 1GAX with [Aminoacyl-tRNA Synthetases]. 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

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