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

Nature Structural & Molecular Biology volume 10, pages 271–279 (2003)Cite this article

Abstract

The crystal structure of the tetrameric α2β2 acetyl-coenzyme A synthase/carbon monoxide dehydrogenase from Moorella thermoacetica has been solved at 1.9 Å resolution. Surprisingly, the two α 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 α 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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Figure 1: Fold of the ACS/CODH αcββαo tetramer in the monoclinic (C2) crystal form.
Figure 2: Structure of the A-clusters in the αc and αo subunits depicted as ball-and-stick models.
Figure 3: Stereo view of a superposition of the Ao- and Ac-clusters.
Figure 4: Stereo views of the structure of the C-cluster in the β subunit.
Figure 5: Proposed catalytic mechanism and schematic representation of the A-clusters.

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Acknowledgements

We thank T. Rabilloud for preparing the NDSB195 reagent and M.Y. Darensbourg for helpful discussion about the feasibility of a Nip0 state. This study was supported by the Robert A. Welch Foundation, the National Institutes of Health and by the CEA and the CNRS through institutional funding. We also thank L. Martin for excellent technical help. We appreciate the help with X-ray data collection from the following scientists working at the European Synchrotron Radiation Facility: L. Jacquamet and M. Pirocchi (LCCP and BM30), J. McCarthy (ID14EH1) and G. Sainz (ID29).

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  1. Claudine Darnault, Anne Volbeda, Eun Jin Kim and Paul A. Lindahl: These two authors contributed equally to this work.

Authors and Affiliations

  1. Laboratoire de Cristallographie et Cristallogenèse des Protéines, Institut de Biologie Structurale 'Jean-Pierre Ebel', CEA, UJF, CNRS, 41, rue Jules Horowitz, Grenoble, 38027, Cedex 1, France

    Claudine Darnault, Anne Volbeda, Pierre Legrand, Xavier Vernède & Juan C. Fontecilla-Camps

  2. Department of Chemistry, Texas A&M University, College Station, Texas, 77843, USA

    Eun Jin Kim & Paul A. Lindahl

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Correspondence to Juan C. Fontecilla-Camps.

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Darnault, C., Volbeda, A., Kim, E. et al. Ni-Zn-[Fe4-S4] and Ni-Ni-[Fe4-S4] clusters in closed and open α subunits of acetyl-CoA synthase/carbon monoxide dehydrogenase. Nat Struct Mol Biol 10, 271–279 (2003). https://doi.org/10.1038/nsb912

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