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| | <StructureSection load='5c0t' size='340' side='right'caption='[[5c0t]], [[Resolution|resolution]] 1.96Å' scene=''> | | <StructureSection load='5c0t' size='340' side='right'caption='[[5c0t]], [[Resolution|resolution]] 1.96Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5c0t]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5C0T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5C0T FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5c0t]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5C0T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5C0T FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3f0p|3f0p]], [[5c0u|5c0u]], [[5c17|5c17]], [[5dsf|5dsf]]</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=5c0t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c0t OCA], [https://pdbe.org/5c0t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5c0t RCSB], [https://www.ebi.ac.uk/pdbsum/5c0t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5c0t ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">merB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alkylmercury_lyase Alkylmercury lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.99.1.2 4.99.1.2] </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=5c0t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c0t OCA], [http://pdbe.org/5c0t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5c0t RCSB], [http://www.ebi.ac.uk/pdbsum/5c0t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5c0t ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/MERB_ECOLX MERB_ECOLX]] Cleaves the carbon-mercury bond of organomercurials such as phenylmercuric acetate. One product is Hg(2+), which is subsequently detoxified by the mercuric reductase (By similarity). | + | [https://www.uniprot.org/uniprot/MERB_ECOLX MERB_ECOLX] Cleaves the carbon-mercury bond of organomercurials such as phenylmercuric acetate. One product is Hg(2+), which is subsequently detoxified by the mercuric reductase (By similarity). |
| | <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: Bacillus coli migula 1895]] | |
| - | [[Category: Alkylmercury lyase]] | |
| - | [[Category: Large Structures]] | |
| - | [[Category: Cappadocia, L]] | |
| - | [[Category: Lafrance-Vanasse, J]] | |
| - | [[Category: Lecoq, L]] | |
| - | [[Category: Mansour, A]] | |
| - | [[Category: Omichinski, J G]] | |
| - | [[Category: Stevenson, M]] | |
| - | [[Category: Sygusch, J]] | |
| - | [[Category: Wahba, H M]] | |
| - | [[Category: Wilcox, D E]] | |
| - | [[Category: Wilkinson, K J]] | |
| - | [[Category: Bacterial protein]] | |
| - | [[Category: Cysteine]] | |
| | [[Category: Escherichia coli]] | | [[Category: Escherichia coli]] |
| - | [[Category: Lyase]] | + | [[Category: Large Structures]] |
| - | [[Category: Mercury]] | + | [[Category: Cappadocia L]] |
| - | [[Category: Metal binding protein]] | + | [[Category: Lafrance-Vanasse J]] |
| - | [[Category: Mutation]] | + | [[Category: Lecoq L]] |
| | + | [[Category: Mansour A]] |
| | + | [[Category: Omichinski JG]] |
| | + | [[Category: Stevenson M]] |
| | + | [[Category: Sygusch J]] |
| | + | [[Category: Wahba HM]] |
| | + | [[Category: Wilcox DE]] |
| | + | [[Category: Wilkinson KJ]] |
| Structural highlights
Function
MERB_ECOLX Cleaves the carbon-mercury bond of organomercurials such as phenylmercuric acetate. One product is Hg(2+), which is subsequently detoxified by the mercuric reductase (By similarity).
Publication Abstract from PubMed
In bacterial resistance to mercury, the organomercurial lyase (MerB) plays a key role in the detoxification pathway through its ability to cleave Hg-carbon bonds. Two cysteines (C96 and C159; Escherichia coli MerB numbering) and an aspartic acid (D99) have been identified as the key catalytic residues, and these three residues are conserved in all but four known MerB variants, where the aspartic acid is replaced by a serine. To understand the role of the active site serine, we characterized the structure and metal-binding properties of an E. coli MerB mutant with a serine substituted for D99 (MerB D99S) as well as one of the native MerB variants containing a serine residue in the active site (Bacillus megaterium MerB2). Surprisingly, the MerB D99S protein co-purified with a bound metal that was determined to be Cu(II) from UV-vis absorption, ICP-MS, NMR and EPR studies. X-ray structural studies revealed that the Cu(II) is bound to the active site cysteine residues of MerB D99S, but that it is displaced following the addition of either an organomercurial substrate or ionic mercury product. In contrast, the B. megaterium MerB2 protein does not co-purify with copper, but the structure of the B. megaterium MerB2-Hg complex is highly similar to the structure of the MerB D99S-Hg complexes. These results demonstrate that the active site aspartic acid is crucial for both the enzymatic activity and metal-binding specificity of MerB proteins and suggest a possible functional relationship between MerB and its only known structural homolog, the copper-binding protein NosL.
Structural and biochemical characterization of a copper-binding mutant of the organomercurial lyase MerB: Insight into the key role of the active site aspartic acid in both Hg-carbon bond cleavage and metal-binding specificity.,Wahba H, Lecoq L, Stevenson MJ, Mansour A, Cappadocia L, Lafrance-Vanasse J, Wilkinson KJ, Sygusch J, Wilcox DE, Omichinski JG Biochemistry. 2016 Jan 28. PMID:26820485[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Wahba H, Lecoq L, Stevenson MJ, Mansour A, Cappadocia L, Lafrance-Vanasse J, Wilkinson KJ, Sygusch J, Wilcox DE, Omichinski JG. Structural and biochemical characterization of a copper-binding mutant of the organomercurial lyase MerB: Insight into the key role of the active site aspartic acid in both Hg-carbon bond cleavage and metal-binding specificity. Biochemistry. 2016 Jan 28. PMID:26820485 doi:http://dx.doi.org/10.1021/acs.biochem.5b01298
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