4qt4: Difference between revisions

<table><tr><td colspan='2'>[[4qt4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pyogenes_NZ131 Streptococcus pyogenes NZ131]. 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 [https://proteopedia.org/fgij/fg.htm?mol=4QT4 FirstGlance]. <br>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4qt4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qt4 OCA], [https://pdbe.org/4qt4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qt4 RCSB], [https://www.ebi.ac.uk/pdbsum/4qt4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qt4 ProSAT]</span></td></tr>

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>

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*[[Peptidyl-tRNA hydrolase|Peptidyl-tRNA hydrolase]]

[[Category: Streptococcus pyogenes NZ131]]