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TitleComparison of Three Methyl-Coenzyme M Reductases from Phylogenetically Distant Organisms: Unusual Amino Acid Modification, Conservation and Adaptation
Journal, issue, pagesJ. Mol. Biol., Vol. 303, Page 329-, Year 2000
Publish dateAug 23, 2000 (structure data deposition date)
AuthorsGrabarse, W. / Mahlert, F. / Shima, S. / Thauer, R.K. / Ermler, U.
External linksJ. Mol. Biol. / PubMed:11023796
MethodsX-ray diffraction
Resolution1.6 - 2.7 Å
Structure data

PDB-1e6v:
Methyl-coenzyme M reductase from Methanopyrus kandleri
Method: X-RAY DIFFRACTION / Resolution: 2.7 Å

PDB-1e6y:
Methyl-coenzyme M reductase from Methanosarcina barkeri
Method: X-RAY DIFFRACTION / Resolution: 1.6 Å

Chemicals

ChemComp-F43:
FACTOR 430

ChemComp-TP7:
Coenzyme B

ChemComp-COM:
1-THIOETHANESULFONIC ACID

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

Source
  • methanopyrus kandleri (archaea)
  • methanosarcina barkeri (archaea)
KeywordsOXIDOREDUCTASE / BIOLOGICAL METHANOGENESIS / NI-ENZYME / NI ENZYME

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