6hzj
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Apo structure of TP domain from clinical penicillin-resistant mutant Neisseria gonorrhoea strain 6140 Penicillin-Binding Protein 2 (PBP2)== | |
| + | <StructureSection load='6hzj' size='340' side='right'caption='[[6hzj]], [[Resolution|resolution]] 1.43Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6hzj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Neisseria_gonorrhoeae_FA6140 Neisseria gonorrhoeae FA6140]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HZJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6HZJ 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]] 1.43Å</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=6hzj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hzj OCA], [https://pdbe.org/6hzj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6hzj RCSB], [https://www.ebi.ac.uk/pdbsum/6hzj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6hzj ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/PBP2_NEIGO PBP2_NEIGO] Synthesis of cross-linked peptidoglycan from the lipid intermediates. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Even with the emergence of antibiotic resistance, penicillin and the wider family of beta-lactams have remained the single most important family of antibiotics. The periplasmic/extra-cytoplasmic targets of penicillin are a family of enzymes with a highly conserved catalytic activity involved in the final stage of bacterial cell wall (peptidoglycan) biosynthesis. Named after their ability to bind penicillin, rather than their catalytic activity, these key targets are called penicillin-binding proteins (PBPs). Resistance is predominantly mediated by reducing the target drug concentration via beta-lactamases; however, naturally transformable bacteria have also acquired target-mediated resistance by inter-species recombination. Here we focus on structural based interpretations of amino acid alterations associated with the emergence of resistance within clinical isolates and include new PBP3 structures along with new, and improved, PBP-beta-lactam co-structures. | ||
| - | + | Novel and Improved Crystal Structures of H. influenzae, E. coli and P. aeruginosa Penicillin-Binding Protein 3 (PBP3) and N. gonorrhoeae PBP2: Toward a Better Understanding of beta-Lactam Target-Mediated Resistance.,Bellini D, Koekemoer L, Newman H, Dowson CG J Mol Biol. 2019 Aug 23;431(18):3501-3519. doi: 10.1016/j.jmb.2019.07.010. Epub, 2019 Jul 10. PMID:31301409<ref>PMID:31301409</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Bellini | + | <div class="pdbe-citations 6hzj" style="background-color:#fffaf0;"></div> |
| - | [[Category: Dowson | + | == References == |
| - | [[Category: | + | <references/> |
| - | [[Category: | + | __TOC__ |
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Neisseria gonorrhoeae FA6140]] | ||
| + | [[Category: Bellini D]] | ||
| + | [[Category: Dowson CG]] | ||
| + | [[Category: Koekemoer L]] | ||
| + | [[Category: Newman H]] | ||
Current revision
Apo structure of TP domain from clinical penicillin-resistant mutant Neisseria gonorrhoea strain 6140 Penicillin-Binding Protein 2 (PBP2)
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