1mjg
From Proteopedia
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CRYSTAL STRUCTURE OF BIFUNCTIONAL CARBON MONOXIDE DEHYDROGENASE/ACETYL-COA SYNTHASE(CODH/ACS) FROM MOORELLA THERMOACETICA (F. CLOSTRIDIUM THERMOACETICUM)
Overview
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.
About this Structure
1MJG is a Protein complex structure of sequences from Moorella thermoacetica with , , , and as ligands. Active as Carbon-monoxide dehydrogenase (acceptor), with EC number 1.2.99.2 Full crystallographic information is available from OCA.
Reference
A Ni-Fe-Cu center in a bifunctional carbon monoxide dehydrogenase/acetyl-CoA synthase., Doukov TI, Iverson TM, Seravalli J, Ragsdale SW, Drennan CL, Science. 2002 Oct 18;298(5593):567-72. PMID:12386327
Page seeded by OCA on Thu Feb 21 13:55:45 2008
Categories: Carbon-monoxide dehydrogenase (acceptor) | Moorella thermoacetica | Protein complex | Doukov, T I. | Drennan, C L. | Iverson, T M. | Ragsdale, S W. | Seravalli, J. | ACT | CU1 | NI | SF4 | XCC | Acetyl-coa synthase (acs) | Carbon monoxide dehydrogenase(codh) | Clostridium thermoaceticum | Electron transfer | Helical domain | Hydrophobic co channel | Nickel-coopper-iron-sulfur (ni-cu-fe-s) cluster | Nickel-iron-sulfur cluster (ni-fe-s) | Rossmann fold | Substrate tunnel | Wood-ljundahl pathway
