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

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

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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Complement C3 Convertase, Alternative Pathway / chemistry*
  • Helix-Turn-Helix Motifs / genetics
  • Hemolysin Proteins / chemistry
  • Kinetics
  • Molecular Sequence Data
  • Nucleic Acids / chemistry
  • Protein Binding
  • Protein Conformation
  • Protein Structure, Tertiary
  • RNA / chemistry*
  • RNA-Binding Proteins / chemistry
  • Sequence Homology, Amino Acid
  • Staphylococcus aureus / metabolism
  • Virulence

Substances

  • Hemolysin Proteins
  • Nucleic Acids
  • RNA-Binding Proteins
  • RNA
  • Complement C3 Convertase, Alternative Pathway

Associated data

  • PDB/3GO5