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- Title
Ni-Zn-[Fe<sub>4</sub>-S<sub>4</sub>] and Ni-Ni-[Fe<sub>4</sub>-S<sub>4</sub>] clusters in closed and open a subunits of acetyl-CoA synthase/carbon monoxide dehydrogenase.
- Authors
Darnault, Claudine; Volbeda, Anne; Kim, Eun Jin; Legrand, Pierre; Vernede, Xavier; Lindahl, Paul A.; Fontecilla-Camps, Juan C.
- Abstract
The crystal structure of the tetrameric a2?2 acetyl-coenzyme A synthase/carbon monoxide dehydrogenase from Moorella thermoacetica has been solved at 1.9 A resolution. Surprisingly, the two a 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 a 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.
- Subjects
ACETYLCOENZYME A; DEHYDROGENASES
- Publication
Nature Structural Biology, 2003, Vol 10, Issue 4, p271
- ISSN
1072-8368
- Publication type
Article
- DOI
10.1038/nsb912