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4yly
From Proteopedia
(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. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4YLY FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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 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=4yly FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yly OCA], [http://pdbe.org/4yly PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4yly RCSB], [http://www.ebi.ac.uk/pdbsum/4yly PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <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> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 4yly" style="background-color:#fffaf0;"></div> | |
| - | [[Category: | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Aminoacyl-tRNA hydrolase]] | ||
[[Category: Li, X]] | [[Category: Li, X]] | ||
[[Category: Song, Y]] | [[Category: Song, Y]] | ||
| + | [[Category: Teng, M K]] | ||
[[Category: Zhang, F]] | [[Category: Zhang, F]] | ||
| - | [[Category: | + | [[Category: Gram-positive]] |
| + | [[Category: Hydrolase]] | ||
Revision as of 02:13, 28 January 2016
Crystal structure of peptidyl-tRNA hydrolase from a Gram-positive bacterium, staphylococcus aureus at 2.25 angstrom resolution
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