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< | ==Crystal Structure of Peptidyl-tRNA hydrolase from Francisella tularensis== | ||
<StructureSection load='3nea' size='340' side='right'caption='[[3nea]], [[Resolution|resolution]] 2.25Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3nea]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Francisella_tularensis_subsp._tularensis Francisella tularensis subsp. tularensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NEA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NEA FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.25Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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=3nea FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nea OCA], [https://pdbe.org/3nea PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3nea RCSB], [https://www.ebi.ac.uk/pdbsum/3nea PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3nea ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/PTH_FRATT PTH_FRATT] 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;"> | |||
== Publication Abstract from PubMed == | |||
The rational design of novel antibiotics for bacteria involves the identification of inhibitors for enzymes involved in essential biochemical pathways in cells. In this study, the cloning, expression, purification, crystallization and structure of the enzyme peptidyl-tRNA hydrolase from Francisella tularensis, the causative agent of tularemia, was performed. The structure of F. tularensis peptidyl-tRNA hydrolase is comparable to those of other bacterial peptidyl-tRNA hydrolases, with most residues in the active site conserved amongst the family. The resultant reagents, structural data and analyses provide essential information for the structure-based design of novel inhibitors for this class of proteins. | |||
Structure of Francisella tularensis peptidyl-tRNA hydrolase.,Clarke TE, Romanov V, Lam R, Gothe SA, Peddi SR, Razumova EB, Lipman RS, Branstrom AA, Chirgadze NY Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Apr 1;67(Pt, 4):446-9. Epub 2011 Mar 26. PMID:21505237<ref>PMID:21505237</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3nea" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Peptidyl-tRNA hydrolase|Peptidyl-tRNA hydrolase]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
[[ | |||
== | |||
< | |||
[[Category: Francisella tularensis subsp. tularensis]] | [[Category: Francisella tularensis subsp. tularensis]] | ||
[[Category: Branstrom | [[Category: Large Structures]] | ||
[[Category: Chirgadze | [[Category: Branstrom AA]] | ||
[[Category: Gothe | [[Category: Chirgadze NY]] | ||
[[Category: Lam | [[Category: Gothe SA]] | ||
[[Category: Lipman | [[Category: Lam R]] | ||
[[Category: McGrath | [[Category: Lipman RS]] | ||
[[Category: Peddi | [[Category: McGrath TE]] | ||
[[Category: Razumova | [[Category: Peddi SR]] | ||
[[Category: Romanov | [[Category: Razumova E]] | ||
[[Category: Romanov V]] | |||
Latest revision as of 12:13, 6 September 2023
Crystal Structure of Peptidyl-tRNA hydrolase from Francisella tularensisCrystal Structure of Peptidyl-tRNA hydrolase from Francisella tularensis
Structural highlights
FunctionPTH_FRATT The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis (By similarity). Publication Abstract from PubMedThe rational design of novel antibiotics for bacteria involves the identification of inhibitors for enzymes involved in essential biochemical pathways in cells. In this study, the cloning, expression, purification, crystallization and structure of the enzyme peptidyl-tRNA hydrolase from Francisella tularensis, the causative agent of tularemia, was performed. The structure of F. tularensis peptidyl-tRNA hydrolase is comparable to those of other bacterial peptidyl-tRNA hydrolases, with most residues in the active site conserved amongst the family. The resultant reagents, structural data and analyses provide essential information for the structure-based design of novel inhibitors for this class of proteins. Structure of Francisella tularensis peptidyl-tRNA hydrolase.,Clarke TE, Romanov V, Lam R, Gothe SA, Peddi SR, Razumova EB, Lipman RS, Branstrom AA, Chirgadze NY Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Apr 1;67(Pt, 4):446-9. Epub 2011 Mar 26. PMID:21505237[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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