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| | <StructureSection load='5df7' size='340' side='right'caption='[[5df7]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='5df7' size='340' side='right'caption='[[5df7]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5df7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DF7 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5DF7 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5df7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DF7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DF7 FirstGlance]. <br> |
| | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=59H:(2R,4S)-5,5-DIMETHYL-2-[(1R)-2-OXO-1-{[(2R)-2-{[(2-OXOIMIDAZOLIDIN-1-YL)CARBONYL]AMINO}-2-PHENYLACETYL]AMINO}ETHYL]-1,3-THIAZOLIDINE-4-CARBOXYLIC+ACID'>59H</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene></td></tr> | | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=59H:(2R,4S)-5,5-DIMETHYL-2-[(1R)-2-OXO-1-{[(2R)-2-{[(2-OXOIMIDAZOLIDIN-1-YL)CARBONYL]AMINO}-2-PHENYLACETYL]AMINO}ETHYL]-1,3-THIAZOLIDINE-4-CARBOXYLIC+ACID'>59H</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4kqo|4kqo]]</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=5df7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5df7 OCA], [https://pdbe.org/5df7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5df7 RCSB], [https://www.ebi.ac.uk/pdbsum/5df7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5df7 ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pbpB, ftsI_2, ERS445055_04698, PAE221_03076, YQ19_27590 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 "Bacillus aeruginosus" (Schroeter 1872) Trevisan 1885])</td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidoglycan_glycosyltransferase Peptidoglycan glycosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.129 2.4.1.129] </span></td></tr>
| + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5df7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5df7 OCA], [http://pdbe.org/5df7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5df7 RCSB], [http://www.ebi.ac.uk/pdbsum/5df7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5df7 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q51504_PSEAI Q51504_PSEAI] |
| | <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: Peptidoglycan glycosyltransferase]] | + | [[Category: Pseudomonas aeruginosa]] |
| - | [[Category: Males, A]] | + | [[Category: Males A]] |
| - | [[Category: Nettleship, J E]] | + | [[Category: Nettleship JE]] |
| - | [[Category: Owens, R J]] | + | [[Category: Owens RJ]] |
| - | [[Category: Ren, J]] | + | [[Category: Ren J]] |
| - | [[Category: Stuart, D I]] | + | [[Category: Stuart DI]] |
| - | [[Category: Acyl-enzyme complex]]
| + | |
| - | [[Category: Azlocillin]]
| + | |
| - | [[Category: Beta-lactam antibiotic]]
| + | |
| - | [[Category: De-acylation]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
Q51504_PSEAI
Publication Abstract from PubMed
Penicillin-binding protein 3 (PBP3) from Pseudomonas aeruginosa is the molecular target of beta-lactam-based antibiotics. Structures of PBP3 in complexes with azlocillin and cefoperazone, which are in clinical use for the treatment of pseudomonad infections, have been determined to 2.0 A resolution. Together with data from other complexes, these structures identify a common set of residues involved in the binding of beta-lactams to PBP3. Comparison of wild-type and an active site mutant (S294A) showed that increased thermal stability of PBP3 following azlocillin binding was entirely due to covalent binding to S294, whereas cefoperazone binding produces some increase in stability without the covalent link. Consistent with this, a third crystal structure was determined in which the hydrolysis product of cefoperazone was noncovalently bound in the active site of PBP3. This is the first structure of a complex between a penicillin-binding protein and cephalosporic acid and may be important in the design of new noncovalent PBP3 inhibitors.
Crystal structures of penicillin-binding protein 3 in complexes with azlocillin and cefoperazone in both acylated and deacylated forms.,Ren J, Nettleship JE, Males A, Stuart DI, Owens RJ FEBS Lett. 2016 Jan;590(2):288-97. doi: 10.1002/1873-3468.12054. Epub 2016 Jan, 23. PMID:26823174[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ren J, Nettleship JE, Males A, Stuart DI, Owens RJ. Crystal structures of penicillin-binding protein 3 in complexes with azlocillin and cefoperazone in both acylated and deacylated forms. FEBS Lett. 2016 Jan;590(2):288-97. doi: 10.1002/1873-3468.12054. Epub 2016 Jan, 23. PMID:26823174 doi:http://dx.doi.org/10.1002/1873-3468.12054
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