3pz0: Difference between revisions
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<StructureSection load='3pz0' size='340' side='right'caption='[[3pz0]], [[Resolution|resolution]] 2.40Å' scene=''> | <StructureSection load='3pz0' size='340' side='right'caption='[[3pz0]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3pz0]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3pz0]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PZ0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PZ0 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | |||
<tr id=' | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3pz0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pz0 OCA], [https://pdbe.org/3pz0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pz0 RCSB], [https://www.ebi.ac.uk/pdbsum/3pz0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pz0 ProSAT]</span></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=3pz0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pz0 OCA], [https://pdbe.org/3pz0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pz0 RCSB], [https://www.ebi.ac.uk/pdbsum/3pz0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pz0 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/SYLA_AQUAE SYLA_AQUAE] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Aquifex aeolicus | [[Category: Aquifex aeolicus]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Liu RJ]] | |||
[[Category: Liu | [[Category: Wang ED]] | ||
[[Category: Wang | |||
Latest revision as of 20:09, 1 November 2023
The crystal structure of AaLeuRS-CP1The crystal structure of AaLeuRS-CP1
Structural highlights
FunctionPublication Abstract from PubMedA large insertion domain called connective peptide 1 (CP1) present in class Ia aminoacyl-tRNA synthetases is responsible for post-transfer editing. Leucyl-tRNA synthetases (LeuRS) from Aquifex aeolicus and Giardia lamblia possess unique 20 and 59 amino acid insertions respectively within the CP1 that are crucial for editing activity. Crystal structures of AaLeuRS-CP1 (2.4A), GlLeuRS-CP1 (2.6A) and the insertion deletion mutant AaLeuRS-CP1-Delta20 (2.5A) were solved to understand the role of these insertions in editing. Both insertions are folded as peripheral motifs located at the opposite side of the active site entrance in CP1 domain. Docking modeling and site-directed mutagenesis showed that the insertions do not interact with the substrates. Results of molecular dynamics simulations show that the intact CP1 is more dynamic than its mutant devoid of the insertion motif. Altogether, the data show a peripheral insertion without a substrate binding site or major structural role in the active site may modulate catalytic function of a protein probably from protein dynamics regulation in two respective LeuRS CP1s. Further results from Pro and Gly mutational analyses intended to reduce or increase protein flexibility are consistent with this hypothesis. Peripheral insertion modulates editing activity of the isolated CP1 domain of leucyl-tRNA synthetase.,Liu RJ, Tan M, Du DH, Xu BS, Eriani G, Wang ED Biochem J. 2011 Aug 5. PMID:21819379[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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