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| | <StructureSection load='2xva' size='340' side='right'caption='[[2xva]], [[Resolution|resolution]] 1.90Å' scene=''> | | <StructureSection load='2xva' size='340' side='right'caption='[[2xva]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2xva]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_mg1655 Escherichia coli mg1655]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XVA OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2XVA FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2xva]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_str._K-12_substr._MG1655 Escherichia coli str. K-12 substr. MG1655]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XVA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XVA FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SFG:SINEFUNGIN'>SFG</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]] 1.9Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2xvm|2xvm]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SFG:SINEFUNGIN'>SFG</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=2xva FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xva OCA], [http://pdbe.org/2xva PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2xva RCSB], [http://www.ebi.ac.uk/pdbsum/2xva PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2xva 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=2xva FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xva OCA], [https://pdbe.org/2xva PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xva RCSB], [https://www.ebi.ac.uk/pdbsum/2xva PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xva ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/TEHB_ECOLI TEHB_ECOLI]] S-adenosyl-L-methionine dependent methyltransferase that catalyzes the methylation of tellurite and is responsible for tellurite resistance when present in high copy number. Can also methylate selenite and selenium dioxide. Is thus able to detoxify different chalcogens. Can not methylate arsenic compounds.<ref>PMID:11053398</ref> <ref>PMID:21244361</ref> | + | [https://www.uniprot.org/uniprot/TEHB_ECOLI TEHB_ECOLI] S-adenosyl-L-methionine dependent methyltransferase that catalyzes the methylation of tellurite and is responsible for tellurite resistance when present in high copy number. Can also methylate selenite and selenium dioxide. Is thus able to detoxify different chalcogens. Can not methylate arsenic compounds.<ref>PMID:11053398</ref> <ref>PMID:21244361</ref> |
| | <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: Escherichia coli mg1655]] | + | [[Category: Escherichia coli str. K-12 substr. MG1655]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Beis, K]] | + | [[Category: Beis K]] |
| - | [[Category: Cameron, A D]] | + | [[Category: Cameron AD]] |
| - | [[Category: Choudhury, H G]] | + | [[Category: Choudhury HG]] |
| - | [[Category: Iwata, S]] | + | [[Category: Iwata S]] |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
TEHB_ECOLI S-adenosyl-L-methionine dependent methyltransferase that catalyzes the methylation of tellurite and is responsible for tellurite resistance when present in high copy number. Can also methylate selenite and selenium dioxide. Is thus able to detoxify different chalcogens. Can not methylate arsenic compounds.[1] [2]
Publication Abstract from PubMed
The oxyanion derivatives of the chalcogens tellurium and selenium are toxic to living organisms even at very low levels. Bacteria have developed mechanisms to overcome their toxicity by methylating them. The structure of the TehB from Escherichia coli has been determined in the presence of the co-factor analogues S-adenosyl-homocysteine (SAH) and sinefungin (non-hydrolysable form of S-adenosyl-L-methionine) at 1.48 A and 1.9 A respectively. Interestingly, our kinetic data show that TehB does not discriminate between selenium or tellurite oxyanions, making it a very powerful detoxifying protein. Analysis of the active site has identified three conserved residues that are capable of binding and orientating the metals for nucleophilic attack, His176, Arg177 and Arg184. Mutagenesis studies revealed that the His176Ala and Arg184Ala mutants retained most of their activity, whereas the Arg177Ala mutant had 65 % of its activity abolished. Based on the structure and kinetic data we propose an SN2 nucleophilic attack reaction mechanism. These data provide the first molecular understanding on the detoxification of chalcogens by bacteria.
Structure and mechanism of the chalcogen detoxifying protein TehB from Escherichia coli.,Choudhury HG, Cameron AD, Iwata S, Beis K Biochem J. 2011 Jan 18. PMID:21244361[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Liu M, Turner RJ, Winstone TL, Saetre A, Dyllick-Brenzinger M, Jickling G, Tari LW, Weiner JH, Taylor DE. Escherichia coli TehB requires S-adenosylmethionine as a cofactor to mediate tellurite resistance. J Bacteriol. 2000 Nov;182(22):6509-13. PMID:11053398
- ↑ Choudhury HG, Cameron AD, Iwata S, Beis K. Structure and mechanism of the chalcogen detoxifying protein TehB from Escherichia coli. Biochem J. 2011 Jan 18. PMID:21244361 doi:10.1042/BJ20102014
- ↑ Choudhury HG, Cameron AD, Iwata S, Beis K. Structure and mechanism of the chalcogen detoxifying protein TehB from Escherichia coli. Biochem J. 2011 Jan 18. PMID:21244361 doi:10.1042/BJ20102014
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