8zpc
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Acinetobacter baumannii Penicillin-Binding Protein 2== | |
| + | <StructureSection load='8zpc' size='340' side='right'caption='[[8zpc]], [[Resolution|resolution]] 3.31Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8zpc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Acinetobacter_baumannii Acinetobacter baumannii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8ZPC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8ZPC 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]] 3.313Å</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=8zpc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8zpc OCA], [https://pdbe.org/8zpc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8zpc RCSB], [https://www.ebi.ac.uk/pdbsum/8zpc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8zpc ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/G1C6X4_ACIBA G1C6X4_ACIBA] Catalyzes cross-linking of the peptidoglycan cell wall.[HAMAP-Rule:MF_02081] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Penicillin-binding protein 2 (PBP2), a vital protein involved in bacterial cell-wall synthesis, serves a target for beta-lactam antibiotics. Acinetobacter baumannii is a pathogen notorious for multidrug resistance; therefore, exploration of PBPs is pivotal in the development of new antimicrobial strategies. In this study, the tertiary structure of PBP2 from A. baumannii (abPBP2) was elucidated using X-ray crystallography. The structural analysis demonstrated notable movement in the head domain, potentially critical for its glycosyltransferase function, suggesting that abPBP2 assumes a fully closed conformation. Our findings offer valuable information for developing novel antimicrobial agents targeting abPBP2 that are applicable in combating multidrug-resistant infections. | ||
| - | + | Fully closed conformation of penicillin-binding protein revealed by structure of PBP2 from Acinetobacter baumannii.,Jang H, Kim CM, Hong E, Park HH Biochem Biophys Res Commun. 2024 Oct 15;729:150368. doi: , 10.1016/j.bbrc.2024.150368. Epub 2024 Jul 6. PMID:38986258<ref>PMID:38986258</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 8zpc" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Acinetobacter baumannii]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Jang HS]] | ||
| + | [[Category: Park HH]] | ||
Current revision
Acinetobacter baumannii Penicillin-Binding Protein 2
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