3CF4
Structure of the CODH component of the M. barkeri ACDS complex
Summary for 3CF4
Entry DOI | 10.2210/pdb3cf4/pdb |
Descriptor | Acetyl-CoA decarboxylase/synthase alpha subunit, Acetyl-CoA decarboxylase/synthase epsilon subunit, IRON/SULFUR CLUSTER, ... (10 entities in total) |
Functional Keywords | methanomicrobia, iron-nikel-sulfur, 4fe-ni-4s, oxidoreductase |
Biological source | Methanosarcina barkeri More |
Total number of polymer chains | 2 |
Total formula weight | 110019.32 |
Authors | Gong, W.,Hao, B.,Wei, Z.,Ferguson Jr., D.J.,Tallant, T.,Krzycki, J.A.,Chan, M.K. (deposition date: 2008-03-01, release date: 2008-07-22, Last modification date: 2024-02-21) |
Primary citation | Gong, W.,Hao, B.,Wei, Z.,Ferguson Jr., D.J.,Tallant, T.,Krzycki, J.A.,Chan, M.K. Structure of the alpha2 epsilon2 Ni-dependent CO dehydrogenase component of the Methanosarcina barkeri acetyl-CoA decarboxylase/synthase complex Proc.Natl.Acad.Sci.USA, 105:9558-9563, 2008 Cited by PubMed Abstract: Ni-dependent carbon monoxide dehydrogenases (Ni-CODHs) are a diverse family of enzymes that catalyze reversible CO:CO(2) oxidoreductase activity in acetogens, methanogens, and some CO-using bacteria. Crystallography of Ni-CODHs from CO-using bacteria and acetogens has revealed the overall fold of the Ni-CODH core and has suggested structures for the C cluster that mediates CO:CO(2) interconversion. Despite these advances, the mechanism of CO oxidation has remained elusive. Herein, we report the structure of a distinct class of Ni-CODH from methanogenic archaea: the alpha(2)epsilon(2) component from the alpha(8)beta(8)gamma(8)delta(8)epsilon(8) CODH/acetyl-CoA decarbonylase/synthase complex, an enzyme responsible for the majority of biogenic methane production on Earth. The structure of this Ni-CODH component provides support for a hitherto unobserved state in which both CO and H(2)O/OH(-) bind to the Ni and the exogenous FCII iron of the C cluster, respectively, and offers insight into the structures and functional roles of the epsilon-subunit and FeS domain not present in nonmethanogenic Ni-CODHs. PubMed: 18621675DOI: 10.1073/pnas.0800415105 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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