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==Crystal structures of Peptidyl-tRNA hydrolase from Mycobacterium tuberculosis - Form 5== | ==Crystal structures of Peptidyl-tRNA hydrolase from Mycobacterium tuberculosis - Form 5== | ||
<StructureSection load='3td2' size='340' side='right' caption='[[3td2]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='3td2' size='340' side='right'caption='[[3td2]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3td2]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3td2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Myctu Myctu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TD2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TD2 FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3tck|3tck]], [[3tcn|3tcn]], [[3td6|3td6]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3tck|3tck]], [[3tcn|3tcn]], [[3td6|3td6]]</div></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MT1042, MTCY10G2.35, pth, Rv1014c ([ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MT1042, MTCY10G2.35, pth, Rv1014c ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83332 MYCTU])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Aminoacyl-tRNA_hydrolase Aminoacyl-tRNA hydrolase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.29 3.1.1.29] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3td2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3td2 OCA], [https://pdbe.org/3td2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3td2 RCSB], [https://www.ebi.ac.uk/pdbsum/3td2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3td2 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/PTH_MYCTU PTH_MYCTU]] The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis (By similarity). | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 28: | Line 28: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Aminoacyl-tRNA hydrolase]] | [[Category: Aminoacyl-tRNA hydrolase]] | ||
[[Category: Large Structures]] | |||
[[Category: Myctu]] | [[Category: Myctu]] | ||
[[Category: Ahmad, R]] | [[Category: Ahmad, R]] | ||
Revision as of 19:52, 6 July 2022
Crystal structures of Peptidyl-tRNA hydrolase from Mycobacterium tuberculosis - Form 5Crystal structures of Peptidyl-tRNA hydrolase from Mycobacterium tuberculosis - Form 5
Structural highlights
Function[PTH_MYCTU] The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis (By similarity). Publication Abstract from PubMedThe X-ray structures of new crystal forms of peptidyl-tRNA hydrolase from M. tuberculosis reported here and the results of previous X-ray studies of the enzyme from different sources provide a picture of the functionally relevant plasticity of the protein molecule. The new X-ray results confirm the connection deduced previously between the closure of the lid at the peptide-binding site and the opening of the gate that separates the peptide-binding and tRNA-binding sites. The plasticity of the molecule indicated by X-ray structures is in general agreement with that deduced from the available solution NMR results. The correlation between the lid and the gate movements is not, however, observed in the NMR structure. Structures of new crystal forms of Mycobacterium tuberculosis peptidyl-tRNA hydrolase and functionally important plasticity of the molecule.,Selvaraj M, Ahmad R, Varshney U, Vijayan M Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Feb 1;68(Pt, 2):124-8. Epub 2012 Jan 21. PMID:22297982[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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