3pot: Difference between revisions
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<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=3pot FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pot OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3pot RCSB], [http://www.ebi.ac.uk/pdbsum/3pot PDBsum]</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=3pot FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pot OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3pot RCSB], [http://www.ebi.ac.uk/pdbsum/3pot PDBsum]</span></td></tr> | ||
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== Function == | |||
[[http://www.uniprot.org/uniprot/MCRA_METTM MCRA_METTM]] Reduction of methyl-coenzyme M (2-(methylthio) ethanesulfonic acid) with 7-mercaptoheptanoylthreonine phosphate to methane and a heterodisulfide. [[http://www.uniprot.org/uniprot/MCRG_METTM MCRG_METTM]] Reduction of methyl-coenzyme M (2-(methylthio) ethanesulfonic acid) with 7-mercaptoheptanoylthreonine phosphate to methane and a heterodisulfide. [[http://www.uniprot.org/uniprot/MCRB_METTM MCRB_METTM]] Reduction of methyl-coenzyme M (2-(methylthio) ethanesulfonic acid) with 7-mercaptoheptanoylthreonine phosphate to methane and a heterodisulfide. | |||
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== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Revision as of 16:13, 25 December 2014
Structural analysis of a Ni(III)-methyl species in methyl-coenzyme M reductase from Methanothermobacter marburgensisStructural analysis of a Ni(III)-methyl species in methyl-coenzyme M reductase from Methanothermobacter marburgensis
Structural highlights
Function[MCRA_METTM] Reduction of methyl-coenzyme M (2-(methylthio) ethanesulfonic acid) with 7-mercaptoheptanoylthreonine phosphate to methane and a heterodisulfide. [MCRG_METTM] Reduction of methyl-coenzyme M (2-(methylthio) ethanesulfonic acid) with 7-mercaptoheptanoylthreonine phosphate to methane and a heterodisulfide. [MCRB_METTM] Reduction of methyl-coenzyme M (2-(methylthio) ethanesulfonic acid) with 7-mercaptoheptanoylthreonine phosphate to methane and a heterodisulfide. Publication Abstract from PubMedWe present the 1.2 A resolution X-ray crystal structure of a Ni-methyl species that is a proposed catalytic intermediate in methyl-coenzyme M reductase (MCR), the enzyme that catalyzes the biological formation of methane. The methyl group is situated 2.1 A proximal of the Ni atom of the MCR coenzyme F(430). A rearrangement of the substrate channel has been posited to bring together substrate species, but Ni(III)-methyl formation alone does not lead to any observable structural changes in the channel. Structural Analysis of a Ni-Methyl Species in Methyl-Coenzyme M Reductase from Methanothermobacter marburgensis.,Cedervall PE, Dey M, Li X, Sarangi R, Hedman B, Ragsdale SW, Wilmot CM J Am Chem Soc. 2011 Mar 25. PMID:21438550[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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