1mro
From Proteopedia
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| - | [[Image:1mro.gif|left|200px]] | + | [[Image:1mro.gif|left|200px]] |
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| - | '''METHYL-COENZYME M REDUCTASE''' | + | {{Structure |
| + | |PDB= 1mro |SIZE=350|CAPTION= <scene name='initialview01'>1mro</scene>, resolution 1.16Å | ||
| + | |SITE= <scene name='pdbsite=F43:Active+Site'>F43</scene> | ||
| + | |LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=F43:FACTOR+430'>F43</scene>, <scene name='pdbligand=TP7:PHOSPHORIC+ACID+N-(1-HYDROXY-7-MERCAPTO-HEPTYL)THREONINE+ESTER'>TP7</scene>, <scene name='pdbligand=COM:1-THIOETHANESULFONIC+ACID'>COM</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''METHYL-COENZYME M REDUCTASE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1MRO is a [ | + | 1MRO is a [[Protein complex]] 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]. |
==Reference== | ==Reference== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9367957 9367957] |
[[Category: Methanothermobacter thermautotrophicus]] | [[Category: Methanothermobacter thermautotrophicus]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:47:22 2008'' |
Revision as of 10:47, 20 March 2008
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| , resolution 1.16Å | |||||||
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| Sites: | |||||||
| Ligands: | , , , , and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
METHYL-COENZYME M REDUCTASE
Overview
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.
About this Structure
1MRO is a Protein complex structure of sequences from Methanothermobacter thermautotrophicus. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Mar 20 12:47:22 2008
Categories: Methanothermobacter thermautotrophicus | Protein complex | Ermler, U. | Grabarse, W. | COM | F43 | GOL | NA | TP7 | ZN | Biological methanogenesis | Ni-enzyme | Oxidoreductase
