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1mro

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Revision as of 06:55, 29 March 2017

METHYL-COENZYME M REDUCTASE

Structural highlights

1mro is a 6 chain structure with sequence from Methanothermobacter marburgensis str. marburg. The November 2014 RCSB PDB Molecule of the Month feature on Methyl-coenzyme M Reductase by David Goodsell is 10.2210/rcsb_pdb/mom_2014_11. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , , , ,
NonStd Res:	, , , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Methyl-coenzyme M reductase (MCR), the enzyme responsible for the microbial formation of methane, is a 300-kilodalton protein organized as a hexamer in an alpha2beta2gamma2 arrangement. The crystal structure of the enzyme from Methanobacterium thermoautotrophicum, determined at 1.45 angstrom resolution for the inactive enzyme state MCRox1-silent, reveals that two molecules of the nickel porphinoid coenzyme F430 are embedded between the subunits alpha, alpha', beta, and gamma and alpha', alpha, beta', and gamma', forming two identical active sites. Each site is accessible for the substrate methyl-coenzyme M through a narrow channel locked after binding of the second substrate coenzyme B. Together with a second structurally characterized enzyme state (MCRsilent) containing the heterodisulfide of coenzymes M and B, a reaction mechanism is proposed that uses a radical intermediate and a nickel organic compound.

Crystal structure of methyl-coenzyme M reductase: the key enzyme of biological methane formation.,Ermler U, Grabarse W, Shima S, Goubeaud M, Thauer RK Science. 1997 Nov 21;278(5342):1457-62. PMID:9367957^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Ermler U, Grabarse W, Shima S, Goubeaud M, Thauer RK. Crystal structure of methyl-coenzyme M reductase: the key enzyme of biological methane formation. Science. 1997 Nov 21;278(5342):1457-62. PMID:9367957

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1mro"

@@ Line 1: / Line 1: @@
 ==METHYL-COENZYME M REDUCTASE==
 <StructureSection load='1mro' size='340' side='right' caption='[[1mro]], [[Resolution|resolution]] 1.16&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=COM:1-THIOETHANESULFONIC+ACID'>COM</scene>, <scene name='pdbligand=F43:FACTOR+430'>F43</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=TP7:COENZYME+B'>TP7</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
 <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=AGM:5-METHYL-ARGININE'>AGM</scene>, <scene name='pdbligand=GL3:THIOGLYCIN'>GL3</scene>, <scene name='pdbligand=MGN:2-METHYL-GLUTAMINE'>MGN</scene>, <scene name='pdbligand=MHS:N1-METHYLATED+HISTIDINE'>MHS</scene>, <scene name='pdbligand=SMC:S-METHYLCYSTEINE'>SMC</scene></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=1mro FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mro OCA], [http://pdbe.org/1mro PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mro RCSB], [http://www.ebi.ac.uk/pdbsum/1mro 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=1mro FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mro OCA], [http://pdbe.org/1mro PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mro RCSB], [http://www.ebi.ac.uk/pdbsum/1mro PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1mro ProSAT]</span></td></tr>
 </table>
 == Function ==

1mro

From Proteopedia

Revision as of 06:55, 29 March 2017

METHYL-COENZYME M REDUCTASE

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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