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1hbn

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[[Image:1hbn.gif|left|200px]]<br />
 
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<applet load="1hbn" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1hbn, resolution 1.16&Aring;" />
 
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'''METHYL-COENZYME M REDUCTASE'''<br />
 
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==Overview==
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==METHYL-COENZYME M REDUCTASE==
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Methyl-coenzyme M reductase (MCR) catalyzes the final reaction of the, energy conserving pathway of methanogenic archaea in which methylcoenzyme, M and coenzyme B are converted to methane and the heterodisulfide, CoM-S-S-CoB. It operates under strictly anaerobic conditions and contains, the nickel porphinoid F430 which is present in the nickel (I) oxidation, state in the active enzyme. The known crystal structures of the inactive, nickel (II) enzyme in complex with coenzyme M and coenzyme B, (MCR-ox1-silent) and in complex with the heterodisulfide CoM-S-S-CoB, (MCR-silent) were now refined at 1.16 A and 1.8 A resolution, respectively. The atomic resolution structure of MCR-ox1-silent describes, the exact geometry of the cofactor F430, of the active site residues and, of the modified amino ... [[http://ispc.weizmann.ac.il/pmbin/getpm?11491299 (full description)]]
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<StructureSection load='1hbn' size='340' side='right'caption='[[1hbn]], [[Resolution|resolution]] 1.16&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1hbn]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanothermobacter_thermautotrophicus Methanothermobacter thermautotrophicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HBN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HBN FirstGlance]. <br>
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1HBN is a [[http://en.wikipedia.org/wiki/Protein_complex Protein complex]] structure of sequences from [[http://en.wikipedia.org/wiki/Methanothermobacter_thermautotrophicus Methanothermobacter thermautotrophicus]] with ZN, MG, NA, CL, F43, TP7, COM and GOL as [[http://en.wikipedia.org/wiki/ligands ligands]]. Structure known Active Sites: AC1, AC2, AC3, AC4, AC5 and AC6. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HBN OCA]].
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.16&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AGM:5-METHYL-ARGININE'>AGM</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=COM:1-THIOETHANESULFONIC+ACID'>COM</scene>, <scene name='pdbligand=F43:FACTOR+430'>F43</scene>, <scene name='pdbligand=GL3:THIOGLYCIN'>GL3</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MGN:2-METHYL-GLUTAMINE'>MGN</scene>, <scene name='pdbligand=MHS:N1-METHYLATED+HISTIDINE'>MHS</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SMC:S-METHYLCYSTEINE'>SMC</scene>, <scene name='pdbligand=TP7:COENZYME+B'>TP7</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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==Reference==
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1hbn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hbn OCA], [https://pdbe.org/1hbn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hbn RCSB], [https://www.ebi.ac.uk/pdbsum/1hbn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hbn ProSAT]</span></td></tr>
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On the mechanism of biological methane formation: structural evidence for conformational changes in methyl-coenzyme M reductase upon substrate binding., Grabarse W, Mahlert F, Duin EC, Goubeaud M, Shima S, Thauer RK, Lamzin V, Ermler U, J Mol Biol. 2001 May 25;309(1):315-30. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11491299 11491299]
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</table>
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== Function ==
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[https://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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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hb/1hbn_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1hbn ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Methanothermobacter thermautotrophicus]]
[[Category: Methanothermobacter thermautotrophicus]]
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[[Category: Protein complex]]
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[[Category: Ermler U]]
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[[Category: Ermler, U.]]
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[[Category: Grabarse W]]
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[[Category: Grabarse, W.]]
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[[Category: CL]]
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[[Category: COM]]
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[[Category: F43]]
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[[Category: GOL]]
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[[Category: MG]]
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[[Category: NA]]
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[[Category: TP7]]
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[[Category: ZN]]
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[[Category: biological methanogenesis]]
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[[Category: methanogenesis]]
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[[Category: ni-enzyme]]
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[[Category: oxidoreductase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 15:34:01 2007''
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Current revision

METHYL-COENZYME M REDUCTASE

PDB ID 1hbn

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