6i1i: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 3: | Line 3: | ||
<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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6I1I FirstGlance]. <br> | <table><tr><td colspan='2'>[[6i1i]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Eco57 Eco57]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6I1I FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=JPP:PIPERACILLIN+(OPEN+FORM)'>JPP</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=JPP:PIPERACILLIN+(OPEN+FORM)'>JPP</scene></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]], [[6hzr|6hzr]]</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]], [[6hzr|6hzr]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ftsI, pbpB, Z0094, ECs0088 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83334 ECO57])</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=6i1i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6i1i OCA], [http://pdbe.org/6i1i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6i1i RCSB], [http://www.ebi.ac.uk/pdbsum/6i1i PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6i1i 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=6i1i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6i1i OCA], [http://pdbe.org/6i1i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6i1i RCSB], [http://www.ebi.ac.uk/pdbsum/6i1i PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6i1i ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/FTSI_ECO57 FTSI_ECO57]] Catalyzes cross-linking of the peptidoglycan cell wall at the division septum.[HAMAP-Rule:MF_02080] | [[http://www.uniprot.org/uniprot/FTSI_ECO57 FTSI_ECO57]] Catalyzes cross-linking of the peptidoglycan cell wall at the division septum.[HAMAP-Rule:MF_02080] | ||
<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> | |||
</div> | |||
<div class="pdbe-citations 6i1i" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Eco57]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Bellini, D]] | [[Category: Bellini, D]] | ||
