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| | <StructureSection load='7ono' size='340' side='right'caption='[[7ono]], [[Resolution|resolution]] 2.30Å' scene=''> | | <StructureSection load='7ono' size='340' side='right'caption='[[7ono]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[7ono]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7ONO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ONO FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7ono]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7ONO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ONO FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TMO:TRIMETHYLAMINE+OXIDE'>TMO</scene></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]] 2.3Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[7onn|7onn]]</div></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=TMO:TRIMETHYLAMINE+OXIDE'>TMO</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ftsI, pbpB, b0084, JW0082 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr> | + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Serine-type_D-Ala-D-Ala_carboxypeptidase Serine-type D-Ala-D-Ala carboxypeptidase], with EC number [https://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'>[https://proteopedia.org/fgij/fg.htm?mol=7ono FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ono OCA], [https://pdbe.org/7ono PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ono RCSB], [https://www.ebi.ac.uk/pdbsum/7ono PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ono ProSAT]</span></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=7ono FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ono OCA], [https://pdbe.org/7ono PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ono RCSB], [https://www.ebi.ac.uk/pdbsum/7ono PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ono 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>
| + | [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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 7ono" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 7ono" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Penicillin-binding protein 3D structures|Penicillin-binding protein 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ecoli]] | + | [[Category: Escherichia coli K-12]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Serine-type D-Ala-D-Ala carboxypeptidase]]
| + | [[Category: Freischem S]] |
| - | [[Category: Freischem, S]] | + | [[Category: Grimm I]] |
| - | [[Category: Grimm, I]] | + | [[Category: Weiergraeber OH]] |
| - | [[Category: Weiergraeber, O H]] | + | |
| - | [[Category: Membrane protein]]
| + | |
| - | [[Category: Pbp3]]
| + | |
| - | [[Category: Peptidoglycan synthesis]]
| + | |
| - | [[Category: Transpeptidase domain]]
| + | |
| Structural highlights
Function
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).[1] [2] [3] [4] [5] [6]
Publication Abstract from PubMed
Novel antimicrobial strategies are urgently required because of the rising threat of multi drug resistant bacterial strains and the infections caused by them. Among the available target structures, the so-called penicillin binding proteins are of particular interest, owing to their good accessibility in the periplasmic space, and the lack of homologous proteins in humans, reducing the risk of side effects of potential drugs. In this report, we focus on the interaction of the innovative beta-lactam antibiotic AIC499 with penicillin binding protein 3 (PBP3) from Escherichia coli and Pseudomonas aeruginosa. This recently developed monobactam displays broad antimicrobial activity, against Gram-negative strains, and improved resistance to most classes of beta-lactamases. By analyzing crystal structures of the respective complexes, we were able to explore the binding mode of AIC499 to its target proteins. In addition, the apo structures determined for PBP3, from P. aeruginosa and the catalytic transpeptidase domain of the E. coli orthologue, provide new insights into the dynamics of these proteins and the impact of drug binding.
Interaction Mode of the Novel Monobactam AIC499 Targeting Penicillin Binding Protein 3 of Gram-Negative Bacteria.,Freischem S, Grimm I, Lopez-Perez A, Willbold D, Klenke B, Vuong C, Dingley AJ, Weiergraber OH Biomolecules. 2021 Jul 19;11(7). pii: biom11071057. doi: 10.3390/biom11071057. PMID:34356681[7]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Spratt BG. Distinct penicillin binding proteins involved in the division, elongation, and shape of Escherichia coli K12. Proc Natl Acad Sci U S A. 1975 Aug;72(8):2999-3003. PMID:1103132
- ↑ Pisabarro AG, Prats R, Vaquez D, Rodriguez-Tebar A. Activity of penicillin-binding protein 3 from Escherichia coli. J Bacteriol. 1986 Oct;168(1):199-206. doi: 10.1128/jb.168.1.199-206.1986. PMID:3531167 doi:http://dx.doi.org/10.1128/jb.168.1.199-206.1986
- ↑ Botta GA, Park JT. Evidence for involvement of penicillin-binding protein 3 in murein synthesis during septation but not during cell elongation. J Bacteriol. 1981 Jan;145(1):333-40. doi: 10.1128/jb.145.1.333-340.1981. PMID:6450748 doi:http://dx.doi.org/10.1128/jb.145.1.333-340.1981
- ↑ Ishino F, Matsuhashi M. Peptidoglycan synthetic enzyme activities of highly purified penicillin-binding protein 3 in Escherichia coli: a septum-forming reaction sequence. Biochem Biophys Res Commun. 1981 Aug 14;101(3):905-11. doi:, 10.1016/0006-291x(81)91835-0. PMID:7030331 doi:http://dx.doi.org/10.1016/0006-291x(81)91835-0
- ↑ Addinall SG, Cao C, Lutkenhaus J. FtsN, a late recruit to the septum in Escherichia coli. Mol Microbiol. 1997 Jul;25(2):303-9. doi: 10.1046/j.1365-2958.1997.4641833.x. PMID:9282742 doi:http://dx.doi.org/10.1046/j.1365-2958.1997.4641833.x
- ↑ Nguyen-Disteche M, Fraipont C, Buddelmeijer N, Nanninga N. The structure and function of Escherichia coli penicillin-binding protein 3. Cell Mol Life Sci. 1998 Apr;54(4):309-16. doi: 10.1007/s000180050157. PMID:9614966 doi:http://dx.doi.org/10.1007/s000180050157
- ↑ Freischem S, Grimm I, Lopez-Perez A, Willbold D, Klenke B, Vuong C, Dingley AJ, Weiergraber OH. Interaction Mode of the Novel Monobactam AIC499 Targeting Penicillin Binding Protein 3 of Gram-Negative Bacteria. Biomolecules. 2021 Jul 19;11(7). pii: biom11071057. doi: 10.3390/biom11071057. PMID:34356681 doi:http://dx.doi.org/10.3390/biom11071057
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