ArticleStructure (London, England : 1993)2010
Structure of a virulence regulatory factor CvfB reveals a novel winged helix RNA binding module.
Article in Structure (London, England : 1993), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 23 citations in OpenAlex.
- Silkworm model of bacterial infection facilitates the identification of lysocin E, a potent, ultra-rapid bactericidal antibiotic.The Journal of antibiotics · 2024Review
- Identification of the RNA-binding domain-containing protein RbpA that acts as a global regulator of the pathogenicity ofVirulence · 2022Article
- S1 Domain RNA-Binding Protein CvfD Is a New Posttranscriptional Regulator That Mediates Cold Sensitivity, Phosphate Transport, and Virulence in Streptococcus pneumoniae D39.Journal of bacteriology · 2020Article
- Genomic Characterization ofFrontiers in microbiology · 2019Article
- Antimicrobial resistance and prevalence of CvfB, SEK and SEQ genes amongExperimental and therapeutic medicine · 2017Article
- Novel Nucleoside Diphosphatase Contributes to Staphylococcus aureus Virulence.The Journal of biological chemistry · 2016Article
- The structure and enzymatic properties of a novel RNase II family enzyme from Deinococcus radiodurans.Journal of molecular biology · 2012Article
- Silkworm apolipophorin protein inhibits Staphylococcus aureus virulence.The Journal of biological chemistry · 2011Article
- The roles of S1 RNA-binding domains in Rrp5's interactions with pre-rRNA.RNA (New York, N.Y.) · 2011Article
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Authors and funding
16 authors at 5 institutions in 2 countries.
Funding
Abstract
CvfB is a conserved regulatory protein important for the virulence of Staphylococcus aureus. We show here that CvfB binds RNA. The crystal structure of the CvfB ortholog from Streptococcus pneumoniae at 1.4 A resolution reveals a unique RNA binding protein that is formed from a concatenation of well-known structural modules that bind nucleic acids: three consecutive S1 RNA binding domains and a winged helix (WH) domain. The third S1 and the WH domains are required for cooperative RNA binding and form a continuous surface that likely contributes to the RNA interaction. The WH domain is critical to CvfB function and contains a unique sequence motif. Thus CvfB represents a novel assembly of modules for binding RNA.
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Registered trials
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