1oao

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spinqualitylabelsall models 1oao, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

NIZN[FE4S4] AND NINI[FE4S4] CLUSTERS IN CLOSED AND OPEN ALPHA SUBUNITS OF ACETYL-COA SYNTHASE/CARBON MONOXIDE DEHYDROGENASE

Overview

The crystal structure of the tetrameric alpha2beta2 acetyl-coenzyme A, synthase/carbon monoxide dehydrogenase from Moorella thermoacetica has, been solved at 1.9 A resolution. Surprisingly, the two alpha subunits, display different (open and closed) conformations. Furthermore, X-ray data, collected from crystals near the absorption edges of several metal ions, indicate that the closed form contains one Zn and one Ni at its active, site metal cluster (A-cluster) in the alpha subunit, whereas the open form, has two Ni ions at the corresponding positions. Alternative metal contents, at the active site have been observed in a recent structure of the same, protein in which A-clusters contained one Cu and one Ni, and in, reconstitution studies of a recombinant apo form of a related acetyl-CoA, synthase. On the basis of our observations along with previously reported, data, we postulate that only the A-clusters containing two Ni ions are, catalytically active.

About this Structure

1OAO 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 Known structural/functional Site: . Full crystallographic information is available from OCA.

Reference

Ni-Zn-[Fe4-S4] and Ni-Ni-[Fe4-S4] clusters in closed and open subunits of acetyl-CoA synthase/carbon monoxide dehydrogenase., Darnault C, Volbeda A, Kim EJ, Legrand P, Vernede X, Lindahl PA, Fontecilla-Camps JC, Nat Struct Biol. 2003 Apr;10(4):271-9. PMID:12627225

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