Journal of the American Chemical Society
ARTICLE
in the electron density map. For the substrate-bound state, the outlier
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with CASTp.74 Structure comparisons were calculated with Dali75 and
SSM.76 Figures were prepared with PyMOL.77 Distances discussed in
the text are the average value between the two independent βγ hetero-
dimers observed in the asymmetric unit. Atomic coordinates and
structure factors have been deposited with the Protein Data Bank
2y8n and r2y8nsf for substrate-free, 2yaj and r2yajsf for substrate-
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’ ASSOCIATED CONTENT
S
Supporting Information. Crystallographic statistics, tables,
b
text, figures, and complete refs 18, 72, and 80. This material is
’ AUTHOR INFORMATION
Corresponding Author
(31) Logan, D. T.; Mulliez, E.; Larsson., K. M.; Bodevin, S.; Atta, M.;
Garnaud, P. E.; Sjoberg, B. M.; Fontecave, M. Proc. Natl. Acad. Sci. U.S.A.
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’ ACKNOWLEDGMENT
(32) Peng, Y.; Veneziano, S. E.; Gillispie, G. D.; Broderick, J. B.
J. Biol. Chem. 2010, 285, 27224–27231.
We are grateful to B. T. Golding (Newcastle University), J.
Stubbe (Massachusetts Institute of Technology), and H. Dobbek
(Humboldt-Universit€at zu Berlin) for helpful discussions. We
also acknowledge all four reviewers for valuable suggestions. We
thank S. Werner (Philipps-Universit€at Marburg) for technical
assistance. This work was supported by the DFG SPP 1319 (B.M.
M., M.F., G.M.U., W.B.), DFG SPP 1071 (M.B., T.S., W.B.),
Elitenetzwerk Bayern (B.M.M., M.F.), and Fonds der Chemische
Industrie (B.M.M., W.B.).
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