4qt4: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4qt4]] is a 2 chain structure. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4q55 4q55]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QT4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QT4 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4qt4]] is a 2 chain structure. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=4q55 4q55]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QT4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QT4 FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4jc4|4jc4]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4jc4|4jc4]]</td></tr> | ||
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aminoacyl-tRNA_hydrolase Aminoacyl-tRNA hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.29 3.1.1.29] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aminoacyl-tRNA_hydrolase Aminoacyl-tRNA hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.29 3.1.1.29] </span></td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4qt4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qt4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4qt4 RCSB], [http://www.ebi.ac.uk/pdbsum/4qt4 PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4qt4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qt4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4qt4 RCSB], [http://www.ebi.ac.uk/pdbsum/4qt4 PDBsum]</span></td></tr> | ||
<table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Peptidyl-tRNA hydrolase (Pth) catalyses the release of tRNA and peptide components from peptidyl-tRNA molecules. Pth from a Gram-positive bacterium Streptococcus pyogenes (SpPth) was cloned, expressed, purified and crystallised. Three-dimensional structure of SpPth was determined by X-ray crystallography at 2.19 A resolution. Structure determination showed that the asymmetric unit of the unit cell contained two crystallographically independent molecules, designated A and B. The superimposition of C(alpha) traces of molecules A and B showed an r.m.s. shift of 0.4 A, indicating that the structures of two crystallographically independent molecules were identical. The polypeptide chain of SpPth adopted an overall alpha/beta conformation. The substrate-binding cleft in SpPth is formed with three loops: the gate loop, Ile91-Leu102; the base loop, Gly108-Gly115; and the lid loop, Gly136-Gly150. Unlike in the structures of Pth from Gram-negative bacteria, the entry to the cleft in the structure of SpPth appeared to be virtually closed. However, the conformations of the active site residues were found to be similar. | |||
Crystal structure of peptidyl-tRNA hydrolase from a Gram-positive bacterium, Streptococcus pyogenes at 2.19 A resolution shows the closed structure of the substrate-binding cleft.,Singh A, Gautam L, Sinha M, Bhushan A, Kaur P, Sharma S, Singh TP FEBS Open Bio. 2014 Oct 22;4:915-22. doi: 10.1016/j.fob.2014.10.010. eCollection , 2014. PMID:25389518<ref>PMID:25389518</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Aminoacyl-tRNA hydrolase]] | [[Category: Aminoacyl-tRNA hydrolase]] | ||
[[Category: Bhushan, A | [[Category: Bhushan, A]] | ||
[[Category: Gautam, L | [[Category: Gautam, L]] | ||
[[Category: Kaur, P | [[Category: Kaur, P]] | ||
[[Category: Sharma, S | [[Category: Sharma, S]] | ||
[[Category: Singh, A | [[Category: Singh, A]] | ||
[[Category: Singh, T P | [[Category: Singh, T P]] | ||
[[Category: Sinha, M | [[Category: Sinha, M]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: Peptidyl-trna]] | [[Category: Peptidyl-trna]] | ||
[[Category: Pth]] | [[Category: Pth]] | ||
