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1mjg

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Revision as of 19:16, 30 March 2008 by OCA (Talk | contribs)
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PDB ID 1mjg

Drag the structure with the mouse to rotate
, resolution 2.2Å
Ligands: , , , ,
Activity: Carbon-monoxide dehydrogenase (acceptor), with EC number 1.2.99.2
Related: 1JQK, 1JJY, 1E9V, 1E2U


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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. 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 Sun Mar 30 22:16:52 2008

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