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| | <StructureSection load='5ctm' size='340' side='right'caption='[[5ctm]], [[Resolution|resolution]] 1.00Å' scene=''> | | <StructureSection load='5ctm' size='340' side='right'caption='[[5ctm]], [[Resolution|resolution]] 1.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5ctm]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_7061 Atcc 7061]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CTM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CTM FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5ctm]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_pumilus Bacillus pumilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CTM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CTM FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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]] 1Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene>, <scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5ctn|5ctn]]</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=5ctm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ctm OCA], [https://pdbe.org/5ctm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ctm RCSB], [https://www.ebi.ac.uk/pdbsum/5ctm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ctm ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BPUM_2340 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1408 ATCC 7061])</td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-lactamase Beta-lactamase], with EC number [http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ctm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ctm OCA], [http://pdbe.org/5ctm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ctm RCSB], [http://www.ebi.ac.uk/pdbsum/5ctm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ctm ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A8FFI9_BACP2 A8FFI9_BACP2] |
| | <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: Atcc 7061]] | + | [[Category: Bacillus pumilus]] |
| - | [[Category: Beta-lactamase]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Smith, C A]] | + | [[Category: Smith CA]] |
| - | [[Category: Vakulenko, S B]] | + | [[Category: Vakulenko SB]] |
| - | [[Category: Hydrolase]]
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| Structural highlights
Function
A8FFI9_BACP2
Publication Abstract from PubMed
Production of beta-lactamases of one of four molecular classes (A, B, C and D) is the major mechanism of bacterial resistance to beta-lactams, the largest class of antibiotics, which have saved countless lives since their inception 70 years ago. Although several hundred efficient class D enzymes have been identified in Gram-negative pathogens over the last four decades, none have been reported in Gram-positive bacteria. Here we demonstrate that efficient class D beta-lactamases capable of hydrolyzing a wide array of beta-lactam substrates are widely disseminated in various species of environmental Gram-positive organisms. Class D enzymes of Gram-positive bacteria have a distinct structural architecture and employ a unique substrate-binding mode that is quite different from that of all currently known class A, C and D beta-lactamases. These enzymes thus constitute a previously unknown reservoir of novel antibiotic-resistance enzymes.
Class D beta-lactamases do exist in Gram-positive bacteria.,Toth M, Antunes NT, Stewart NK, Frase H, Bhattacharya M, Smith CA, Vakulenko SB Nat Chem Biol. 2015 Nov 9. doi: 10.1038/nchembio.1950. PMID:26551395[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Toth M, Antunes NT, Stewart NK, Frase H, Bhattacharya M, Smith CA, Vakulenko SB. Class D beta-lactamases do exist in Gram-positive bacteria. Nat Chem Biol. 2015 Nov 9. doi: 10.1038/nchembio.1950. PMID:26551395 doi:http://dx.doi.org/10.1038/nchembio.1950
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