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| | <StructureSection load='6t5k' size='340' side='right'caption='[[6t5k]], [[Resolution|resolution]] 1.33Å' scene=''> | | <StructureSection load='6t5k' size='340' side='right'caption='[[6t5k]], [[Resolution|resolution]] 1.33Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6t5k]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Dsm_17526 Dsm 17526]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6T5K OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6T5K FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6t5k]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Echinicola_vietnamensis Echinicola vietnamensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6T5K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6T5K FirstGlance]. <br> |
| - | </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=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]] 1.33Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Echvi_2632 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=390884 DSM 17526])</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=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=6t5k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6t5k OCA], [http://pdbe.org/6t5k PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6t5k RCSB], [http://www.ebi.ac.uk/pdbsum/6t5k PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6t5k 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=6t5k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6t5k OCA], [https://pdbe.org/6t5k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6t5k RCSB], [https://www.ebi.ac.uk/pdbsum/6t5k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6t5k ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/L0FY79_ECHVK L0FY79_ECHVK] |
| | <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: Dsm 17526]] | + | [[Category: Echinicola vietnamensis]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Frohlich, C]] | + | [[Category: Frohlich C]] |
| - | [[Category: Antimicrobial protein]]
| + | |
| - | [[Category: Beta-lactamase]]
| + | |
| - | [[Category: Carbapenemase]]
| + | |
| - | [[Category: Environmental]]
| + | |
| Structural highlights
Function
L0FY79_ECHVK
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.
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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