1mjg

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Revision as of 19:20, 20 November 2007

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spinqualitylabelsall models 1mjg, resolution 2.2Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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 CU1, NI, ACT, SF4 and XCC 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

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