1MJG

CRYSTAL STRUCTURE OF BIFUNCTIONAL CARBON MONOXIDE DEHYDROGENASE/ACETYL-COA SYNTHASE(CODH/ACS) FROM MOORELLA THERMOACETICA (F. CLOSTRIDIUM THERMOACETICUM)

Summary for 1MJG

• Entry DOI: 10.2210/pdb1mjg/pdb
• Related: 1E2U 1E9V 1JJY 1JQK
• Descriptor: CARBON MONOXIDE DEHYDROGENASE BETA SUBUNIT, Carbon monoxide dehydrogenase alpha subunit, IRON/SULFUR CLUSTER, ... (8 entities in total)
• Functional Keywords: carbon monoxide dehydrogenase(codh), acetyl-coa synthase (acs), nickel-iron-sulfur cluster (ni-fe-s), nickel-coopper-iron-sulfur (ni-cu-fe-s) cluster, hydrophobic co channel, substrate tunnel, helical domain, rossmann fold, electron transfer, clostridium thermoaceticum, wood-ljundahl pathway, oxidoreductase
• Biological source: Moorella thermoacetica; More
• Total number of polymer chains: 8
• Total formula weight: 624897.83

Authors

Doukov, T.I.,Iverson, T.M.,Seravalli, J.,Ragsdale, S.W.,Drennan, C.L. (deposition date: 2002-08-27, release date: 2003-01-28, Last modification date: 2019-11-20)

Primary citation

Doukov, T.I.,Iverson, T.M.,Seravalli, J.,Ragsdale, S.W.,Drennan, C.L.
A Ni-Fe-Cu center in a bifunctional carbon monoxide dehydrogenase/acetyl-CoA synthase
Science, 298:567-572, 2002

PubMed Abstract: A metallocofactor containing iron, sulfur, copper, and nickel has been discovered in the enzyme carbon monoxide dehydrogenase/acetyl-CoA (coenzyme A) synthase from Moorella thermoacetica (f. Clostridium thermoaceticum). Our structure at 2.2 angstrom resolution reveals that the cofactor responsible for the assembly of acetyl-CoA contains a [Fe4S4] cubane bridged to a copper-nickel binuclear site. The presence of these three metals together in one cluster was unanticipated and suggests a newly discovered role for copper in biology. The different active sites of this bifunctional enzyme complex are connected via a channel, 138 angstroms long, that provides a conduit for carbon monoxide generated at the C-cluster on one subunit to be incorporated into acetyl-CoA at the A-cluster on the other subunit.

PubMed: 12386327
DOI: 10.1126/science.1075843

Experimental method

X-RAY DIFFRACTION (2.2 Å)