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| | <StructureSection load='3w8k' size='340' side='right'caption='[[3w8k]], [[Resolution|resolution]] 1.50Å' scene=''> | | <StructureSection load='3w8k' size='340' side='right'caption='[[3w8k]], [[Resolution|resolution]] 1.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3w8k]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_pneumoniae"_(schroeter_1886)_flugge_1886 "bacillus pneumoniae" (schroeter 1886) flugge 1886]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3W8K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3W8K FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3w8k]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Klebsiella_pneumoniae Klebsiella pneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3W8K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3W8K FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 1.5Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">blaMOX-1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=573 "Bacillus pneumoniae" (Schroeter 1886) Flugge 1886])</td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Beta-lactamase Beta-lactamase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.6 3.5.2.6] </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=3w8k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3w8k OCA], [https://pdbe.org/3w8k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3w8k RCSB], [https://www.ebi.ac.uk/pdbsum/3w8k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3w8k 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=3w8k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3w8k OCA], [https://pdbe.org/3w8k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3w8k RCSB], [https://www.ebi.ac.uk/pdbsum/3w8k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3w8k ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q51578_KLEPN Q51578_KLEPN] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Beta-lactamase]] | + | [[Category: Klebsiella pneumoniae]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Furuyama, T]] | + | [[Category: Furuyama T]] |
| - | [[Category: Ishii, Y]] | + | [[Category: Ishii Y]] |
| - | [[Category: Oguri, T]] | + | [[Category: Oguri T]] |
| - | [[Category: Shimizu-ibuka, A]] | + | [[Category: Shimizu-ibuka A]] |
| - | [[Category: Antibiotic resistance]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| Structural highlights
Function
Q51578_KLEPN
Publication Abstract from PubMed
Mox-1 is a unique plasmid-mediated class C beta-lactamase that hydrolyzes penicillins, cephalothin, and the expanded-spectrum cephalosporins cefepime and moxalactam. In order to understand the unique substrate profile of this enzyme, we determined the X-ray crystallographic structure of Mox-1 beta-lactamase at a 1.5-A resolution. The overall structure of Mox-1 beta-lactamase resembles that of other AmpC enzymes, with some notable exceptions. First, comparison with other enzymes whose structures have been solved reveals significant differences in the composition of amino acids that make up the hydrogen-bonding network and the position of structural elements in the substrate-binding cavity. Second, the main-chain electron density is not observed in two regions, one containing amino acid residues 214 to 216 positioned in the Omega loop and the other in the N terminus of the B3 beta-strand corresponding to amino acid residues 303 to 306. The last two observations suggest that there is significant structural flexibility of these regions, a property which may impact the recognition and binding of substrates in Mox-1. These important differences allow us to propose that the binding of moxalactam in Mox-1 is facilitated by the avoidance of steric clashes, indicating that a substrate-induced conformational change underlies the basis of the hydrolytic profile of Mox-1 beta-lactamase.
Crystal structure of Mox-1, a unique plasmid-mediated class C beta-lactamase with hydrolytic activity towards moxalactam.,Oguri T, Furuyama T, Okuno T, Ishii Y, Tateda K, Bonomo RA, Shimizu-Ibuka A Antimicrob Agents Chemother. 2014 Jul;58(7):3914-20. doi: 10.1128/AAC.02363-13., Epub 2014 Apr 28. PMID:24777102[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Oguri T, Furuyama T, Okuno T, Ishii Y, Tateda K, Bonomo RA, Shimizu-Ibuka A. Crystal structure of Mox-1, a unique plasmid-mediated class C beta-lactamase with hydrolytic activity towards moxalactam. Antimicrob Agents Chemother. 2014 Jul;58(7):3914-20. doi: 10.1128/AAC.02363-13., Epub 2014 Apr 28. PMID:24777102 doi:http://dx.doi.org/10.1128/AAC.02363-13
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