7nu0: Difference between revisions
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==Crystal Structure of Neisseria gonorrhoeae LeuRS L550A mutant in Complex with ATP and L-leucinol== | |||
<StructureSection load='7nu0' size='340' side='right'caption='[[7nu0]], [[Resolution|resolution]] 1.89Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7nu0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Neisseria_gonorrhoeae Neisseria gonorrhoeae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7NU0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7NU0 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=DCL:2-AMINO-4-METHYL-PENTAN-1-OL'>DCL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=7nu0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7nu0 OCA], [https://pdbe.org/7nu0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7nu0 RCSB], [https://www.ebi.ac.uk/pdbsum/7nu0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7nu0 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[https://www.uniprot.org/uniprot/SYL_NEIG2 SYL_NEIG2]] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
To correctly aminoacylate tRNA(Leu), leucyl-tRNA synthetase (LeuRS) catalyzes three reactions: activation of leucine by ATP to form leucyl-adenylate (Leu-AMP), transfer of this amino acid to tRNA(Leu) and post-transfer editing of any mischarged product. Although LeuRS has been well characterized biochemically, detailed structural information is currently only available for the latter two stages of catalysis. We have solved crystal structures for all enzymatic states of Neisseria gonorrhoeae LeuRS during Leu-AMP formation. These show a cycle of dramatic conformational changes, involving multiple domains, and correlate with an energetically unfavorable peptide-plane flip observed in the active site of the pre-transition state structure. Biochemical analyses, combined with mutant structural studies, reveal that this backbone distortion acts as a trigger, temporally compartmentalizing the first two catalytic steps. These results unveil the remarkable effect of this small structural alteration on the global dynamics and activity of the enzyme. | |||
Partitioning of the initial catalytic steps of leucyl-tRNA synthetase is driven by an active site peptide-plane flip.,Pang L, Zanki V, Strelkov SV, Van Aerschot A, Gruic-Sovulj I, Weeks SD Commun Biol. 2022 Aug 29;5(1):883. doi: 10.1038/s42003-022-03825-8. PMID:36038645<ref>PMID:36038645</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Pang | <div class="pdbe-citations 7nu0" style="background-color:#fffaf0;"></div> | ||
[[Category: Strelkov | == References == | ||
[[Category: Weeks | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Neisseria gonorrhoeae]] | |||
[[Category: Pang L]] | |||
[[Category: Strelkov SV]] | |||
[[Category: Weeks SD]] | |||
Revision as of 09:11, 28 September 2022
Crystal Structure of Neisseria gonorrhoeae LeuRS L550A mutant in Complex with ATP and L-leucinolCrystal Structure of Neisseria gonorrhoeae LeuRS L550A mutant in Complex with ATP and L-leucinol
Structural highlights
FunctionPublication Abstract from PubMedTo correctly aminoacylate tRNA(Leu), leucyl-tRNA synthetase (LeuRS) catalyzes three reactions: activation of leucine by ATP to form leucyl-adenylate (Leu-AMP), transfer of this amino acid to tRNA(Leu) and post-transfer editing of any mischarged product. Although LeuRS has been well characterized biochemically, detailed structural information is currently only available for the latter two stages of catalysis. We have solved crystal structures for all enzymatic states of Neisseria gonorrhoeae LeuRS during Leu-AMP formation. These show a cycle of dramatic conformational changes, involving multiple domains, and correlate with an energetically unfavorable peptide-plane flip observed in the active site of the pre-transition state structure. Biochemical analyses, combined with mutant structural studies, reveal that this backbone distortion acts as a trigger, temporally compartmentalizing the first two catalytic steps. These results unveil the remarkable effect of this small structural alteration on the global dynamics and activity of the enzyme. Partitioning of the initial catalytic steps of leucyl-tRNA synthetase is driven by an active site peptide-plane flip.,Pang L, Zanki V, Strelkov SV, Van Aerschot A, Gruic-Sovulj I, Weeks SD Commun Biol. 2022 Aug 29;5(1):883. doi: 10.1038/s42003-022-03825-8. PMID:36038645[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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