2v0g: Difference between revisions

Latest revision as of 15:00, 13 December 2023

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.

Structural highlights

2v0g is a 4 chain structure with sequence from Thermus thermophilus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 3.5Å
Ligands:	ANZ, HG, LEU, SO4, ZN
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q7SIE4_THETH

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ 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. An antifungal agent inhibits an aminoacyl-tRNA synthetase by trapping tRNA in the editing site. Science. 2007 Jun 22;316(5832):1759-61. PMID:17588934 doi:https://dx.doi.org/316/5832/1759

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] 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. An antifungal agent inhibits an aminoacyl-tRNA synthetase by trapping tRNA in the editing site. Science. 2007 Jun 22;316(5832):1759-61. PMID:17588934 doi:https://dx.doi.org/316/5832/1759

[1]

@@ Line 3: / Line 3: @@
 <StructureSection load='2v0g' size='340' side='right'caption='[[2v0g]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2v0g]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/"flavobacterium_thermophilum"_yoshida_and_oshima_1971 "flavobacterium thermophilum" yoshida and oshima 1971]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V0G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2V0G FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2v0g]] is a 4 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2V0G FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene>, <scene name='pdbligand=LEU:LEUCINE'>LEU</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.5&#8491;</td></tr>
-<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ANZ:[(6-AMINO-9H-PURIN-9-YL)-[5-FLUORO-1,3-DIHYDRO-1-HYDROXY-2,1-BENZOXABOROLE]-4YL]METHYL+DIHYDROGEN+PHOSPHATE'>ANZ</scene></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANZ:[(6-AMINO-9H-PURIN-9-YL)-[5-FLUORO-1,3-DIHYDRO-1-HYDROXY-2,1-BENZOXABOROLE]-4YL]METHYL+DIHYDROGEN+PHOSPHATE'>ANZ</scene>, <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene>, <scene name='pdbligand=LEU:LEUCINE'>LEU</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1h3n|1h3n]], [[1obc|1obc]], [[1obh|1obh]], [[2bte|2bte]], [[2byt|2byt]], [[2v0c|2v0c]]</div></td></tr>
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2v0g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v0g OCA], [https://pdbe.org/2v0g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2v0g RCSB], [https://www.ebi.ac.uk/pdbsum/2v0g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2v0g ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/Q7SIE4_THETH Q7SIE4_THETH]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 36: / Line 37: @@
 __TOC__
 </StructureSection>
-[[Category: Flavobacterium thermophilum yoshida and oshima 1971]]
 [[Category: Large Structures]]
-[[Category: Akama, T]]
+[[Category: Thermus thermophilus]]
-[[Category: Alley, M R.K]]
+[[Category: Akama T]]
-[[Category: Baker, S]]
+[[Category: Alley MRK]]
-[[Category: Benkovic, S J]]
+[[Category: Baker S]]
-[[Category: Crepin, T]]
+[[Category: Benkovic SJ]]
-[[Category: Cusack, S]]
+[[Category: Crepin T]]
-[[Category: Hernandez, V]]
+[[Category: Cusack S]]
-[[Category: Mao, W]]
+[[Category: Hernandez V]]
-[[Category: Martinis, S A]]
+[[Category: Mao W]]
-[[Category: Plattner, J]]
+[[Category: Martinis SA]]
-[[Category: Rock, F]]
+[[Category: Plattner J]]
-[[Category: Shapiro, L]]
+[[Category: Rock F]]
-[[Category: Tukalo, M]]
+[[Category: Shapiro L]]
-[[Category: Yaremchuk, A]]
+[[Category: Tukalo M]]
-[[Category: Zhang, Y]]
+[[Category: Yaremchuk A]]
-[[Category: Zhou, H]]
+[[Category: Zhang Y]]
-[[Category: Aminoacyl-trna synthetase]]
+[[Category: Zhou H]]
-[[Category: Atp-binding]]
-[[Category: Class i aminoacyl- trna synthetase]]
-[[Category: Editing]]
-[[Category: Ligase]]
-[[Category: Metal-binding]]
-[[Category: Nucleotide-binding zinc]]
-[[Category: Protein biosynthesis]]
-[[Category: Synthetase]]

2v0g: Difference between revisions

Latest revision as of 15:00, 13 December 2023

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.

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

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