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| | <StructureSection load='6hzj' size='340' side='right'caption='[[6hzj]], [[Resolution|resolution]] 1.43Å' scene=''> | | <StructureSection load='6hzj' size='340' side='right'caption='[[6hzj]], [[Resolution|resolution]] 1.43Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6hzj]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6HZJ FirstGlance]. <br> | + | <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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6hzh|6hzh]], [[6hzi|6hzi]], [[4u3t|4u3t]]</td></tr> | + | </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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">penA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=528353 Neisseria gonorrhoeae FA6140])</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> |
| - | <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=6hzj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hzj OCA], [http://pdbe.org/6hzj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6hzj RCSB], [http://www.ebi.ac.uk/pdbsum/6hzj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6hzj ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/E5KLA8_NEIGO E5KLA8_NEIGO]] Catalyzes cross-linking of the peptidoglycan cell wall at the division septum.[HAMAP-Rule:MF_02080] | + | [https://www.uniprot.org/uniprot/PBP2_NEIGO PBP2_NEIGO] Synthesis of cross-linked peptidoglycan from the lipid intermediates. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Neisseria gonorrhoeae fa6140]] | + | [[Category: Neisseria gonorrhoeae FA6140]] |
| - | [[Category: Serine-type D-Ala-D-Ala carboxypeptidase]]
| + | [[Category: Bellini D]] |
| - | [[Category: Bellini, D]] | + | [[Category: Dowson CG]] |
| - | [[Category: Dowson, C G]] | + | [[Category: Koekemoer L]] |
| - | [[Category: Koekemoer, L]] | + | [[Category: Newman H]] |
| - | [[Category: Newman, H]] | + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Penicillin-binding protein]]
| + | |
| - | [[Category: Transpeptidase]]
| + | |
| Structural highlights
Function
PBP2_NEIGO Synthesis of cross-linked peptidoglycan from the lipid intermediates.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Bellini D, Koekemoer L, Newman H, Dowson CG. 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. J Mol Biol. 2019 Aug 23;431(18):3501-3519. doi: 10.1016/j.jmb.2019.07.010. Epub, 2019 Jul 10. PMID:31301409 doi:http://dx.doi.org/10.1016/j.jmb.2019.07.010
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