2v0g

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[[Image:2v0g.gif|left|200px]]<br /><applet load="2v0g" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2v0g.gif|left|200px]]
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caption="2v0g, resolution 3.50&Aring;" />
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'''LEUCYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS COMPLEXED WITH A TRNA(LEU) TRANSCRIPT WITH 5-FLUORO-1,3-DIHYDRO-1-HYDROXY-2,1-BENZOXABOROLE (AN2690) FORMING AN ADDUCT TO THE RIBOSE OF ADENOSINE-76 IN THE ENZYME EDITING SITE.'''<br />
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{{Structure
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|PDB= 2v0g |SIZE=350|CAPTION= <scene name='initialview01'>2v0g</scene>, resolution 3.50&Aring;
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|SITE= <scene name='pdbsite=AC1:LEU+Binding+Site+For+Chain+D'>AC1</scene>
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|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=LEU:LEUCINE'>LEU</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''LEUCYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS COMPLEXED WITH A TRNA(LEU) TRANSCRIPT WITH 5-FLUORO-1,3-DIHYDRO-1-HYDROXY-2,1-BENZOXABOROLE (AN2690) FORMING AN ADDUCT TO THE RIBOSE OF ADENOSINE-76 IN THE ENZYME EDITING SITE.'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2V0G is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=HG:'>HG</scene>, <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=LEU:'>LEU</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:LEU+Binding+Site+For+Chain+D'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V0G OCA].
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2V0G is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V0G OCA].
==Reference==
==Reference==
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An antifungal agent inhibits an aminoacyl-tRNA synthetase by trapping tRNA in the editing site., Rock FL, Mao W, Yaremchuk A, Tukalo M, Crepin T, Zhou H, Zhang YK, Hernandez V, Akama T, Baker SJ, Plattner JJ, Shapiro L, Martinis SA, Benkovic SJ, Cusack S, Alley MR, Science. 2007 Jun 22;316(5832):1759-61. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17588934 17588934]
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An antifungal agent inhibits an aminoacyl-tRNA synthetase by trapping tRNA in the editing site., Rock FL, Mao W, Yaremchuk A, Tukalo M, Crepin T, Zhou H, Zhang YK, Hernandez V, Akama T, Baker SJ, Plattner JJ, Shapiro L, Martinis SA, Benkovic SJ, Cusack S, Alley MR, Science. 2007 Jun 22;316(5832):1759-61. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17588934 17588934]
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Thermus thermophilus]]
[[Category: Thermus thermophilus]]
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[[Category: synthetase]]
[[Category: synthetase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:52:09 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:41:57 2008''

Revision as of 16:41, 20 March 2008

Image:2v0g.gif


PDB ID 2v0g

Drag the structure with the mouse to rotate
, resolution 3.50Å
Sites:
Ligands: , , and
Coordinates: save as pdb, mmCIF, xml



LEUCYL-TRNA SYNTHETASE FROM THERMUS THERMOPHILUS COMPLEXED WITH A TRNA(LEU) TRANSCRIPT WITH 5-FLUORO-1,3-DIHYDRO-1-HYDROXY-2,1-BENZOXABOROLE (AN2690) FORMING AN ADDUCT TO THE RIBOSE OF ADENOSINE-76 IN THE ENZYME EDITING SITE.


Overview

Aminoacyl-transfer RNA (tRNA) synthetases, which catalyze the attachment of the correct amino acid to its corresponding tRNA during translation of the genetic code, are proven antimicrobial drug targets. We show that the broad-spectrum antifungal 5-fluoro-1,3-dihydro-1-hydroxy-2,1-benzoxaborole (AN2690), in development for the treatment of onychomycosis, inhibits yeast cytoplasmic leucyl-tRNA synthetase by formation of a stable tRNA(Leu)-AN2690 adduct in the editing site of the enzyme. Adduct formation is mediated through the boron atom of AN2690 and the 2'- and 3'-oxygen atoms of tRNA's3'-terminal adenosine. The trapping of enzyme-bound tRNA(Leu) in the editing site prevents catalytic turnover, thus inhibiting synthesis of leucyl-tRNA(Leu) and consequentially blocking protein synthesis. This result establishes the editing site as a bona fide target for aminoacyl-tRNA synthetase inhibitors.

About this Structure

2V0G is a Protein complex structure of sequences from Thermus thermophilus. Full crystallographic information is available from OCA.

Reference

An antifungal agent inhibits an aminoacyl-tRNA synthetase by trapping tRNA in the editing site., Rock FL, Mao W, Yaremchuk A, Tukalo M, Crepin T, Zhou H, Zhang YK, Hernandez V, Akama T, Baker SJ, Plattner JJ, Shapiro L, Martinis SA, Benkovic SJ, Cusack S, Alley MR, Science. 2007 Jun 22;316(5832):1759-61. PMID:17588934

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