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1OAO

NiZn[Fe4S4] and NiNi[Fe4S4] clusters in closed and open alpha subunits of acetyl-CoA synthase/carbon monoxide dehydrogenase

Summary for 1OAO
Entry DOI10.2210/pdb1oao/pdb
Related1JJY 1JQK 1MJG
DescriptorCARBON MONOXIDE DEHYDROGENASE/ACETYL-COA SYNTHASE SUBUNIT BETA, ZINC ION, NICKEL (II) ION, ... (14 entities in total)
Functional Keywordsoxidoreductase-transferase complex, electron transfer, oxidoreductase, acetyl-coa formation, wood/ljungdahl pathway, nickel, oxidoreductase/transferase
Biological sourceMOORELLA THERMOACETICA
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Total number of polymer chains4
Total formula weight316522.65
Authors
Darnault, C.,Volbeda, A.,Kim, E.J.,Legrand, P.,Vernede, X.,Lindahl, P.A.,Fontecilla-Camps, J.C. (deposition date: 2003-01-20, release date: 2003-04-11, Last modification date: 2025-10-01)
Primary citationDarnault, C.,Volbeda, A.,Kim, E.J.,Legrand, P.,Vernede, X.,Lindahl, P.A.,Fontecilla-Camps, J.C.
Ni-Zn-[Fe4-S4] and Ni-Ni-[Fe4-S4] Clusters in Closed and Open Alpha Subunits of Acetyl-Coa Synthase/Carbon Monoxide Dehydrogenase
Nat.Struct.Biol., 10:271-, 2003
Cited by
PubMed Abstract: 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.
PubMed: 12627225
DOI: 10.1038/NSB912
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.9 Å)
Structure validation

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