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| - | [[Image:1e6y.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1e6y| PDB=1e6y | SCENE= }} | | {{STRUCTURE_1e6y| PDB=1e6y | SCENE= }} |
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| - | '''METHYL-COENZYME M REDUCTASE FROM METHANOSARCINA BARKERI'''
| + | ===METHYL-COENZYME M REDUCTASE FROM METHANOSARCINA BARKERI=== |
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| - | ==Overview==
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| - | The nickel enzyme methyl-coenzyme M reductase (MCR) catalyzes the terminal step of methane formation in the energy metabolism of all methanogenic archaea. In this reaction methyl-coenzyme M and coenzyme B are converted to methane and the heterodisulfide of coenzyme M and coenzyme B. The crystal structures of methyl-coenzyme M reductase from Methanosarcina barkeri (growth temperature optimum, 37 degrees C) and Methanopyrus kandleri (growth temperature optimum, 98 degrees C) were determined and compared with the known structure of MCR from Methanobacterium thermoautotrophicum (growth temperature optimum, 65 degrees C). The active sites of MCR from M. barkeri and M. kandleri were almost identical to that of M. thermoautotrophicum and predominantly occupied by coenzyme M and coenzyme B. The electron density at 1.6 A resolution of the M. barkeri enzyme revealed that four of the five modified amino acid residues of MCR from M. thermoautotrophicum, namely a thiopeptide, an S-methylcysteine, a 1-N-methylhistidine and a 5-methylarginine were also present. Analysis of the environment of the unusual amino acid residues near the active site indicates that some of the modifications may be required for the enzyme to be catalytically effective. In M. thermoautotrophicum and M. kandleri high temperature adaptation is coupled with increasing intracellular concentrations of lyotropic salts. This was reflected in a higher fraction of glutamate residues at the protein surface of the thermophilic enzymes adapted to high intracellular salt concentrations. | + | The line below this paragraph, {{ABSTRACT_PUBMED_11023796}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 11023796 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_11023796}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Ni-enzyme]] | | [[Category: Ni-enzyme]] |
| | [[Category: Oxidoreductase]] | | [[Category: Oxidoreductase]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:44:34 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 00:15:20 2008'' |
Revision as of 21:15, 30 June 2008
Template:STRUCTURE 1e6y
METHYL-COENZYME M REDUCTASE FROM METHANOSARCINA BARKERI
Template:ABSTRACT PUBMED 11023796
About this Structure
1E6Y is a Protein complex structure of sequences from Methanosarcina barkeri. Full crystallographic information is available from OCA.
Reference
Comparison of three methyl-coenzyme M reductases from phylogenetically distant organisms: unusual amino acid modification, conservation and adaptation., Grabarse W, Mahlert F, Shima S, Thauer RK, Ermler U, J Mol Biol. 2000 Oct 20;303(2):329-44. PMID:11023796
Page seeded by OCA on Tue Jul 1 00:15:20 2008
