6hzr
From Proteopedia
(Difference between revisions)
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<StructureSection load='6hzr' size='340' side='right'caption='[[6hzr]], [[Resolution|resolution]] 1.19Å' scene=''> | <StructureSection load='6hzr' size='340' side='right'caption='[[6hzr]], [[Resolution|resolution]] 1.19Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6hzr]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HZR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6HZR FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6hzr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseae Pseae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HZR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6HZR FirstGlance]. <br> |
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6hzh|6hzh]], [[6hzi|6hzi]], [[6hzj|6hzj]], [[6hzo|6hzo]], [[6hzq|6hzq]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6hzh|6hzh]], [[6hzi|6hzi]], [[6hzj|6hzj]], [[6hzo|6hzo]], [[6hzq|6hzq]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ftsI, pbpB, PA4418 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=208964 PSEAE])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Serine-type_D-Ala-D-Ala_carboxypeptidase Serine-type D-Ala-D-Ala carboxypeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.16.4 3.4.16.4] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Serine-type_D-Ala-D-Ala_carboxypeptidase Serine-type D-Ala-D-Ala carboxypeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.16.4 3.4.16.4] </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=6hzr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hzr OCA], [http://pdbe.org/6hzr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6hzr RCSB], [http://www.ebi.ac.uk/pdbsum/6hzr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6hzr ProSAT]</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=6hzr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hzr OCA], [http://pdbe.org/6hzr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6hzr RCSB], [http://www.ebi.ac.uk/pdbsum/6hzr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6hzr ProSAT]</span></td></tr> | ||
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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/FTSI_PSEAE FTSI_PSEAE]] Catalyzes cross-linking of the peptidoglycan cell wall at the division septum (By similarity). Binds penicillin (PubMed:20580675).[HAMAP-Rule:MF_02080]<ref>PMID:20580675</ref> | [[http://www.uniprot.org/uniprot/FTSI_PSEAE FTSI_PSEAE]] Catalyzes cross-linking of the peptidoglycan cell wall at the division septum (By similarity). Binds penicillin (PubMed:20580675).[HAMAP-Rule:MF_02080]<ref>PMID:20580675</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. | ||
| + | |||
| + | 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 6hzr" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| + | [[Category: Pseae]] | ||
[[Category: Serine-type D-Ala-D-Ala carboxypeptidase]] | [[Category: Serine-type D-Ala-D-Ala carboxypeptidase]] | ||
[[Category: Bellini, D]] | [[Category: Bellini, D]] | ||
Revision as of 07:22, 19 February 2020
Apo structure of Pseudomonas aeruginosa Penicillin-Binding Protein 3
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