4yly: Difference between revisions
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==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]] 2.25Å' 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]] 2.25Å</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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 4yly" style="background-color:#fffaf0;"></div> | ||
[[Category: | |||
[[Category: | ==See Also== | ||
[[Category: Zhang | *[[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]] | |||
Latest revision as of 15:36, 8 November 2023
Crystal structure of peptidyl-tRNA hydrolase from a Gram-positive bacterium, staphylococcus aureus at 2.25 angstrom resolution
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