1mro: Difference between revisions

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{{Seed}}
[[Image:1mro.png|left|200px]]


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==METHYL-COENZYME M REDUCTASE==
The line below this paragraph, containing "STRUCTURE_1mro", creates the "Structure Box" on the page.
<StructureSection load='1mro' size='340' side='right'caption='[[1mro]], [[Resolution|resolution]] 1.16&Aring;' scene=''>
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== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1mro]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanothermobacter_marburgensis_str._Marburg Methanothermobacter marburgensis str. Marburg]. The November 2014 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Methyl-coenzyme M Reductase''  by David Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2014_11 10.2210/rcsb_pdb/mom_2014_11]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MRO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MRO FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</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=COM:1-THIOETHANESULFONIC+ACID'>COM</scene>, <scene name='pdbligand=GL3:THIOGLYCIN'>GL3</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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>
{{STRUCTURE_1mro|  PDB=1mro  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1mro FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mro OCA], [https://pdbe.org/1mro PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mro RCSB], [https://www.ebi.ac.uk/pdbsum/1mro PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mro ProSAT]</span></td></tr>
</table>
== Function ==
[https://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.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mr/1mro_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1mro ConSurf].
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== 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.


===METHYL-COENZYME M REDUCTASE===
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<ref>PMID:9367957</ref>


 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
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<references/>
{{ABSTRACT_PUBMED_9367957}}
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</StructureSection>
==About this Structure==
[[Category: Large Structures]]
1MRO is a 6 chains structure of sequences from [http://en.wikipedia.org/wiki/Methanothermobacter_thermautotrophicus Methanothermobacter thermautotrophicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MRO OCA].
[[Category: Methanothermobacter marburgensis str. Marburg]]
 
[[Category: Methyl-coenzyme M Reductase]]
==Reference==
[[Category: RCSB PDB Molecule of the Month]]
<ref group="xtra">PMID:9367957</ref><references group="xtra"/>
[[Category: Ermler U]]
[[Category: Methanothermobacter thermautotrophicus]]
[[Category: Grabarse W]]
[[Category: Ermler, U.]]
[[Category: Grabarse, W.]]
[[Category: Biological methanogenesis]]
[[Category: Ni-enzyme]]
[[Category: Oxidoreductase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 16:31:53 2009''
Retrieved from "https://proteopedia.org/1mro"