@article{f154fd5f4d6441f59e7cd3de03aa9f5c,
title = "Structure of a Virulence Regulatory Factor CvfB Reveals a Novel Winged Helix RNA Binding Module",
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 {\AA} 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 = "Microbio, Proteins, RNA",
author = "Yasuhiko Matsumoto and Qingping Xu and Shinya Miyazaki and Chikara Kaito and Farr, {Carol L.} and Axelrod, {Herbert L.} and Chiu, {Hsiu Ju} and Klock, {Heath E.} and Knuth, {Mark W.} and Miller, {Mitchell D.} and Elsliger, {Marc Andr{\'e}} and Deacon, {Ashley M.} and Adam Godzik and Lesley, {Scott A.} and Kazuhisa Sekimizu and Wilson, {Ian A.}",
note = "Funding Information: We thank all the members of the JCSG for their general contributions to the protein production and structural work. We also thank K. Hiramatsu (Juntendo University, Tokyo, Japan) and N. Ogasawara (Nara Institute of Science and Technology, Nara, Japan) for reagents. The project is sponsored by the National Institutes of Health (NIH), National Institute of General Medical Sciences (NIGMS) Protein Structure Initiative (U54 GM074898 to the JCSG), by a Grant-in-Aid for Scientific Research (Japan) (21022015, 20790057, 20390021), and also in part by the Program for Promotion of Fundamental Studies in Health Sciences of the National Institute of Biomedical Innovation (Japan) and Genome Pharmaceuticals Institute Co., Ltd. (Tokyo, Japan). Portions of this research were carried out at the Stanford Synchrotron Radiation Lightsource (SSRL). SSRL is a national user facility operated by Stanford University on behalf of the U.S. Department of Energy/Office of Basic Energy Sciences. The content is solely the responsibility of the authors and does not necessarily represent the official views of NIGMS or NIH. ",
year = "2010",
month = mar,
doi = "10.1016/j.str.2010.02.007",
language = "English",
volume = "18",
pages = "537--547",
journal = "Structure",
issn = "0969-2126",
publisher = "Cell Press",
number = "4",
}