Ni-Zn-[Fe4-S4] and Ni-Ni-[Fe4-S4] clusters in closed and open α subunits of acetyl-CoA synthase/carbon monoxide dehydrogenase View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2003-04

AUTHORS

Claudine Darnault, Anne Volbeda, Eun Jin Kim, Pierre Legrand, Xavier Vernède, Paul A. Lindahl, Juan C. Fontecilla-Camps

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. More... »

PAGES

271-279

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/nsb912

DOI

http://dx.doi.org/10.1038/nsb912

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1021021826

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/12627225


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