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| | <StructureSection load='6t5l' size='340' side='right'caption='[[6t5l]], [[Resolution|resolution]] 2.17Å' scene=''> | | <StructureSection load='6t5l' size='340' side='right'caption='[[6t5l]], [[Resolution|resolution]] 2.17Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6t5l]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Ccug_39352 Ccug 39352]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6T5L OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6T5L FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6t5l]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Myroides_odoratimimus Myroides odoratimimus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6T5L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6T5L FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 2.17Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AS202_20055 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=76832 CCUG 39352])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=6t5l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6t5l OCA], [http://pdbe.org/6t5l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6t5l RCSB], [http://www.ebi.ac.uk/pdbsum/6t5l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6t5l 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=6t5l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6t5l OCA], [https://pdbe.org/6t5l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6t5l RCSB], [https://www.ebi.ac.uk/pdbsum/6t5l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6t5l ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A0A0U3H0V9_9FLAO A0A0U3H0V9_9FLAO] |
| | <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 6t5l" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6t5l" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ccug 39352]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Frohlich, C]] | + | [[Category: Myroides odoratimimus]] |
| - | [[Category: Antimicrobial protein]] | + | [[Category: Frohlich C]] |
| - | [[Category: Beta-lactamase]]
| + | |
| - | [[Category: Carbapenemase]]
| + | |
| - | [[Category: Environmental]]
| + | |
| - | [[Category: Mbl]]
| + | |
| - | [[Category: Metallo-beta-lactamase]]
| + | |
| Structural highlights
Function
A0A0U3H0V9_9FLAO
Publication Abstract from PubMed
BACKGROUND: MBLs form a large and heterogeneous group of bacterial enzymes conferring resistance to beta-lactam antibiotics, including carbapenems. A large environmental reservoir of MBLs has been identified, which can act as a source for transfer into human pathogens. Therefore, structural investigation of environmental and clinically rare MBLs can give new insights into structure-activity relationships to explore the role of catalytic and second shell residues, which are under selective pressure. OBJECTIVES: To investigate the structure and activity of the environmental subclass B1 MBLs MYO-1, SHD-1 and ECV-1. METHODS: The respective genes of these MBLs were cloned into vectors and expressed in Escherichia coli. Purified enzymes were characterized with respect to their catalytic efficiency (kcat/Km). The enzymatic activities and MICs were determined for a panel of different beta-lactams, including penicillins, cephalosporins and carbapenems. Thermostability was measured and structures were solved using X-ray crystallography (MYO-1 and ECV-1) or generated by homology modelling (SHD-1). RESULTS: Expression of the environmental MBLs in E. coli resulted in the characteristic MBL profile, not affecting aztreonam susceptibility and decreasing susceptibility to carbapenems, cephalosporins and penicillins. The purified enzymes showed variable catalytic activity in the order of <5% to approximately 70% compared with the clinically widespread NDM-1. The thermostability of ECV-1 and SHD-1 was up to 8 degrees C higher than that of MYO-1 and NDM-1. Using solved structures and molecular modelling, we identified differences in their second shell composition, possibly responsible for their relatively low hydrolytic activity. CONCLUSIONS: These results show the importance of environmental species acting as reservoirs for MBL-encoding genes.
Structural and biochemical characterization of the environmental MBLs MYO-1, ECV-1 and SHD-1.,Frohlich C, Sorum V, Huber S, Samuelsen O, Berglund F, Kristiansson E, Kotsakis SD, Marathe NP, Larsson DGJ, Leiros HS J Antimicrob Chemother. 2020 May 28. pii: 5848379. doi: 10.1093/jac/dkaa175. PMID:32464640[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Frohlich C, Sorum V, Huber S, Samuelsen O, Berglund F, Kristiansson E, Kotsakis SD, Marathe NP, Larsson DGJ, Leiros HS. Structural and biochemical characterization of the environmental MBLs MYO-1, ECV-1 and SHD-1. J Antimicrob Chemother. 2020 May 28. pii: 5848379. doi: 10.1093/jac/dkaa175. PMID:32464640 doi:http://dx.doi.org/10.1093/jac/dkaa175
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