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Protein Science (2007), 16:1285-1293. Published by Cold Spring Harbor Laboratory Press. Copyright © 2007 The Protein Society
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The 2.2 Å resolution crystal structure of Bacillus cereus Nif3-family protein YqfO reveals a conserved dimetal-binding motif and a regulatory domain

Michael H. Godsey1,5, George Minasov2,5, Ludmilla Shuvalova2, Joseph S. Brunzelle3, Ivan I. Vorontsov2, Frank R. Collart4, and Wayne F. Anderson2

1 College of Theology, Arts and Sciences, Concordia University, Portland, Oregon 97211, USA
2 Molecular Pharmacology and Biological Chemistry, Feinberg School of Medicine, Northwestern University, Chicago, Illinois 60611, USA
3 LS-CAT, Advanced Photon Source, Argonne National Laboratory, Argonne, Illinois 60439, USA
4 Midwest Center for Structural Genomics, Argonne National Laboratory, Argonne, Illinois 60439, USA

(RECEIVED November 21, 2006; FINAL REVISION March 6, 2007; ACCEPTED March 7, 2007)

YqfO of Bacillus cereus is a member of the widespread Nif3 family of proteins, which has been highlighted as an important target for structural genomics. The N- and C-terminal domains are conserved across the family and contain a dimetal-binding motif in a putative active site. YqfO contains an insert in the middle of the protein, present in a minority of bacterial family members. The structure of YqfO was determined at a resolution of 2.2 Å and reveals conservation of the putative active site. It also reveals the previously unknown structure of the insert, which despite extremely limited sequence conservation, bears great similarity to PII, CutA, and a number of other trimeric regulatory proteins. Our results suggest that this domain acts as a signal sensor to regulate the still-unknown catalytic activity of the more-conserved domains.

Keywords: structural genomics; Nif3; dimetal; cocatalytic site; PII; CutA; YqfO


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I. I. Vorontsov, G. Minasov, J. S. Brunzelle, L. Shuvalova, O. Kiryukhina, F. R. Collart, and W. F. Anderson
Crystal structure of an apo form of Shigella flexneri ArsH protein with an NADPH-dependent FMN reductase activity
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