This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

4qt4

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Current revision

Crystal structure of Peptidyl-tRNA hydrolase from a Gram-positive bacterium, Streptococcus pyogenes at 2.19 Angstrom resolution shows the Closed Structure of the Substrate Binding Cleft

Structural highlights

4qt4 is a 2 chain structure with sequence from Streptococcus pyogenes NZ131. This structure supersedes the now removed PDB entry 4q55. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.19Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PTH_STRPZ The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis (By similarity).

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Singh A, Gautam L, Sinha M, Bhushan A, Kaur P, Sharma S, Singh TP. 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. FEBS Open Bio. 2014 Oct 22;4:915-22. doi: 10.1016/j.fob.2014.10.010. eCollection , 2014. PMID:25389518 doi:http://dx.doi.org/10.1016/j.fob.2014.10.010

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4qt4"

@@ Line 4: / Line 4: @@
 == Structural highlights ==
 <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>
-</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=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>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.19&#8491;</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=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>
 </table>
 == Function ==

4qt4

From Proteopedia

Current revision

Crystal structure of Peptidyl-tRNA hydrolase from a Gram-positive bacterium, Streptococcus pyogenes at 2.19 Angstrom resolution shows the Closed Structure of the Substrate Binding Cleft

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox