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Structure. 2010 Mar 14;18(4):537-47. doi: 10.1016/j.str.2010.02.007.

Structure of a virulence regulatory factor CvfB reveals a novel winged helix RNA binding module.

Author information

1
Laboratory of Microbiology, Graduate School of Pharmaceutical Sciences, The University of Tokyo, Tokyo 113-0033, Japan.

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.

KEYWORDS:

CvfB; RNA binding; S1 domain; Winged-helix domain; virulence

PMID:
20399190
PMCID:
PMC2858061
DOI:
10.1016/j.str.2010.02.007
[Indexed for MEDLINE]
Free PMC Article

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