Journal
NATURE STRUCTURAL BIOLOGY
Volume 10, Issue 4, Pages 271-279Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsb912
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The crystal structure of the tetrameric alpha(2)beta(2) acetyl-coenzyme A synthase/carbon monoxide dehydrogenase from Moorella thermoacetica has been solved at 1.9 Angstrom resolution. Surprisingly, the two 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 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.
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