ArticleProtein science : a publication of the Protein Society2007
The 2.2 A resolution crystal structure of Bacillus cereus Nif3-family protein YqfO reveals a conserved dimetal-binding motif and a regulatory domain.
Article in Protein science : a publication of the Protein Society, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 23 citations in OpenAlex.
- RNA-seq analysis identified glucose-responsive genes and YqfO as a global regulator in Bacillus subtilis.BMC research notes · 2021Article
- Comparative Genomic Analysis of the DUF34 Protein Family Suggests Role as a Metal Ion Chaperone or Insertase.Biomolecules · 2021Article
- Article
- The Nif3-Family Protein YqfO03 fromInternational journal of molecular sciences · 2018Article
- Switching specific biomolecular interactions on surfaces under complex biological conditions.The Analyst · 2014Article
- Crystal structure of a conserved hypothetical protein MJ0927 from Methanocaldococcus jannaschii reveals a novel quaternary assembly in the Nif3 family.BioMed research international · 2014Article
- A proteomic approach provides new insights into the control of soil-borne plant pathogens by Bacillus species.PloS one · 2013Article
- Insights into the mechanism of type I dehydroquinate dehydratases from structures of reaction intermediates.The Journal of biological chemistry · 2011Article
- Archaeal ubiquitin-like proteins: functional versatility and putative ancestral involvement in tRNA modification revealed by comparative genomic analysis.Archaea (Vancouver, B.C.) · 2010Article
- Structure of putative CutA1 from Homo sapiens determined at 2.05 A resolution.Acta crystallographica. Section F, Structural biology and crystallization communications · 2008Article
- Crystal structure of an apo form of Shigella flexneri ArsH protein with an NADPH-dependent FMN reductase activity.Protein science : a publication of the Protein Society · 2007Article
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7 authors at 3 institutions in 1 country.
Funding
Abstract
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 A 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.
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