1e6v
From Proteopedia
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| - | [[Image:1e6v.jpg|left|200px]]<br /><applet load="1e6v" size=" | + | [[Image:1e6v.jpg|left|200px]]<br /><applet load="1e6v" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1e6v, resolution 2.70Å" /> | caption="1e6v, resolution 2.70Å" /> | ||
'''METHYL-COENZYME M REDUCTASE FROM METHANOPYRUS KANDLERI'''<br /> | '''METHYL-COENZYME M REDUCTASE FROM METHANOPYRUS KANDLERI'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1E6V is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Methanopyrus_kandleri Methanopyrus kandleri] with F43, TP7 and COM as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Sites: <scene name='pdbsite=AC1:F43 Binding Site For Chain A The Subunits D, E, F Contri ...'>AC1</scene>, <scene name='pdbsite=AC2:Tp7 Binding Site For Chain A Symmetry Related Subunits C ...'>AC2</scene>, <scene name='pdbsite=AC3:Com Binding Site For Chain A Symmetry Related Subunits C ...'>AC3</scene>, <scene name='pdbsite=AC4:F43 Binding Site For Chain D The Subunits A, B, C Contri ...'>AC4</scene>, <scene name='pdbsite=AC5:Tp7 Binding Site For Chain D Symmetry Related Subunits C ...'>AC5</scene> and <scene name='pdbsite=AC6:Com Binding Site For Chain D Symmetry Related Subunits C ...'>AC6</scene>. Full crystallographic information is available from [http:// | + | 1E6V is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Methanopyrus_kandleri Methanopyrus kandleri] with <scene name='pdbligand=F43:'>F43</scene>, <scene name='pdbligand=TP7:'>TP7</scene> and <scene name='pdbligand=COM:'>COM</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Sites: <scene name='pdbsite=AC1:F43+Binding+Site+For+Chain+A+The+Subunits+D,+E,+F+Contri+...'>AC1</scene>, <scene name='pdbsite=AC2:Tp7+Binding+Site+For+Chain+A+Symmetry+Related+Subunits+C+...'>AC2</scene>, <scene name='pdbsite=AC3:Com+Binding+Site+For+Chain+A+Symmetry+Related+Subunits+C+...'>AC3</scene>, <scene name='pdbsite=AC4:F43+Binding+Site+For+Chain+D+The+Subunits+A,+B,+C+Contri+...'>AC4</scene>, <scene name='pdbsite=AC5:Tp7+Binding+Site+For+Chain+D+Symmetry+Related+Subunits+C+...'>AC5</scene> and <scene name='pdbsite=AC6:Com+Binding+Site+For+Chain+D+Symmetry+Related+Subunits+C+...'>AC6</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E6V OCA]. |
==Reference== | ==Reference== | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:37:45 2008'' |
Revision as of 07:37, 3 February 2008
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METHYL-COENZYME M REDUCTASE FROM METHANOPYRUS KANDLERI
Overview
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.
About this Structure
1E6V is a Protein complex structure of sequences from Methanopyrus kandleri with , and as ligands. Known structural/functional Sites: , , , , and . 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
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