Structure of a virulence regulatory factor CvfB reveals a novel winged helix RNA binding module.
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.
Matsumoto
Yasuhiko
Y
Laboratory of Microbiology, Graduate School of Pharmaceutical Sciences, The University of Tokyo, Tokyo 113-0033, Japan.
Xu
Qingping
Q
Miyazaki
Shinya
S
Kaito
Chikara
C
Farr
Carol L
CL
Axelrod
Herbert L
HL
Chiu
Hsiu-Ju
HJ
Klock
Heath E
HE
Knuth
Mark W
MW
Miller
Mitchell D
MD
Elsliger
Marc-André
MA
Deacon
Ashley M
AM
Godzik
Adam
A
Lesley
Scott A
SA
Sekimizu
Kazuhisa
K
Wilson
Ian A
IA
D000595:Amino Acid Sequence; D051561:Complement C3 Convertase, Alternative Pathway / Q000737:chemistry*; D019077:Helix-Turn-Helix Motifs / Q000235:genetics; D006460:Hemolysin Proteins / Q000737:chemistry; D007700:Kinetics; D008969:Molecular Sequence Data; D009696:Nucleic Acids / Q000737:chemistry; D011485:Protein Binding; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D012313:RNA / Q000737:chemistry*; D016601:RNA-Binding Proteins / Q000737:chemistry; D017386:Sequence Homology, Amino Acid; D013211:Staphylococcus aureus / Q000378:metabolism; D014774:Virulence
D006460:Hemolysin Proteins; D009696:Nucleic Acids; D016601:RNA-Binding Proteins; D012313:RNA; D051561:Complement C3 Convertase, Alternative Pathway
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