6i1i
From Proteopedia
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<StructureSection load='6i1i' size='340' side='right'caption='[[6i1i]], [[Resolution|resolution]] 1.75Å' scene=''> | <StructureSection load='6i1i' size='340' side='right'caption='[[6i1i]], [[Resolution|resolution]] 1.75Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6i1i]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6I1I OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[6i1i]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_O157:H7 Escherichia coli O157:H7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6I1I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6I1I FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=JPP:PIPERACILLIN+(OPEN+FORM)'>JPP</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6i1i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6i1i OCA], [https://pdbe.org/6i1i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6i1i RCSB], [https://www.ebi.ac.uk/pdbsum/6i1i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6i1i ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/FTSI_ECOLI FTSI_ECOLI] Essential cell division protein that catalyzes cross-linking of the peptidoglycan cell wall at the division septum (PubMed:1103132, PubMed:6450748, PubMed:9614966, PubMed:3531167, PubMed:7030331). Required for localization of FtsN (PubMed:9282742).<ref>PMID:1103132</ref> <ref>PMID:3531167</ref> <ref>PMID:6450748</ref> <ref>PMID:7030331</ref> <ref>PMID:9282742</ref> <ref>PMID:9614966</ref> |
| + | <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. | ||
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| + | 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> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6i1i" style="background-color:#fffaf0;"></div> | ||
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| + | ==See Also== | ||
| + | *[[Penicillin-binding protein 3D structures|Penicillin-binding protein 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Escherichia coli O157:H7]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Bellini | + | [[Category: Bellini D]] |
| - | [[Category: Dowson | + | [[Category: Dowson CG]] |
| - | [[Category: Koekemoer | + | [[Category: Koekemoer L]] |
| - | [[Category: Newman | + | [[Category: Newman H]] |
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Current revision
Crystal structure of TP domain from Escherichia coli penicillin-binding protein 3 in complex with penicillin
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