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1mro

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[[Image:1mro.gif|left|200px]]
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{{Seed}}
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[[Image:1mro.png|left|200px]]
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{{STRUCTURE_1mro| PDB=1mro | SCENE= }}
{{STRUCTURE_1mro| PDB=1mro | SCENE= }}
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'''METHYL-COENZYME M REDUCTASE'''
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===METHYL-COENZYME M REDUCTASE===
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==Overview==
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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.
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The line below this paragraph, {{ABSTRACT_PUBMED_9367957}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 9367957 is the PubMed ID number.
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{{ABSTRACT_PUBMED_9367957}}
==About this Structure==
==About this Structure==
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[[Category: Ni-enzyme]]
[[Category: Ni-enzyme]]
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 01:38:25 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 19:44:43 2008''

Revision as of 16:44, 27 July 2008

Image:1mro.png

Template:STRUCTURE 1mro

METHYL-COENZYME M REDUCTASE

Template:ABSTRACT PUBMED 9367957

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 Sun Jul 27 19:44:43 2008

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