View source for 4yly


==Crystal structure of peptidyl-tRNA hydrolase from a Gram-positive bacterium, staphylococcus aureus at 2.25 angstrom resolution==
<StructureSection load='4yly' size='340' side='right'caption='[[4yly]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4yly]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YLY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YLY 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]] 2.25&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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=4yly FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yly OCA], [https://pdbe.org/4yly PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4yly RCSB], [https://www.ebi.ac.uk/pdbsum/4yly PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4yly ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PTH_STAAU PTH_STAAU] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Peptidyl-tRNA hydrolase (Pth) catalyzes the release of tRNA to relieve peptidyl-tRNA accumulation. Because Pth activity is essential for the viability of bacteria, Pth is regarded as a promising target for the discovery of new antimicrobial agents. Here, the structure of Pth from the Gram-positive bacterium Staphylococcus aureus (SaPth) was solved by X-ray crystallography at a 2.25 A resolution. The SaPth structure exhibits significant structural similarity with other members of the Pth superfamily, with a conserved alpha/beta/alpha sandwich fold. A molecular phylogenetic analysis and a structure database search indicated that SaPth is most similar to its homolog in Streptococcus pyogenes, but it has a different substrate-binding cleft state.

Crystal structure of Staphylococcus aureus peptidyl-tRNA hydrolase at a 2.25 A resolution.,Zhang F, Song Y, Niu L, Teng M, Li X Acta Biochim Biophys Sin (Shanghai). 2015 Dec;47(12):1005-10. doi:, 10.1093/abbs/gmv114. Epub 2015 Oct 26. PMID:26508479<ref>PMID:26508479</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4yly" style="background-color:#fffaf0;"></div>

==See Also==
*[[Peptidyl-tRNA hydrolase|Peptidyl-tRNA hydrolase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Staphylococcus aureus]]
[[Category: Li X]]
[[Category: Song Y]]
[[Category: Teng MK]]
[[Category: Zhang F]]