1mjg | pdb_00001mjg

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

File:1mjg.gif

spinqualitylabelsall models 1mjg, resolution 2.2Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D

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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