The 2.2 Aa resolution crystal structure of Bacillus cereus Nif3-family protein YqfO reveals a conserved dimetal-binding motif and a regulatory domain

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 inse...

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Bibliographic Details
Published in:Protein science 2007-07, Vol.16 (7), p.1285-1293
Main Authors: Godsey, Michael H, Minasov, George, Shuvalova, Ludmilla, Brunzelle, Joseph S, Vorontsov, Ivan I, Collart, Frank R, Anderson, Wayne F
Format: Article
Language:English
Subjects:
Bacillus cereus
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Summary: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 Aa 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.
ISSN:0961-8368