3GO5

Crystal structure of a multidomain protein with nucleic acid binding domains (sp_0946) from streptococcus pneumoniae tigr4 at 1.40 A resolution

Summary for 3GO5

• Entry DOI: 10.2210/pdb3go5/pdb
• Descriptor: Multidomain protein with S1 RNA-binding domains, CHLORIDE ION, 1,2-ETHANEDIOL, ... (4 entities in total)
• Functional Keywords: s1 rna-binding domain, structural genomics, joint center for structural genomics, jcsg, protein structure initiative, psi-2, gene regulation
• Biological source: Streptococcus pneumoniae
• Total number of polymer chains: 1
• Total formula weight: 33546.42

Authors

Joint Center for Structural Genomics (JCSG) (deposition date: 2009-03-18, release date: 2009-04-07, Last modification date: 2024-11-27)

Primary citation

Matsumoto, Y.,Xu, Q.,Miyazaki, S.,Kaito, C.,Farr, C.L.,Axelrod, H.L.,Chiu, H.J.,Klock, H.E.,Knuth, M.W.,Miller, M.D.,Elsliger, M.A.,Deacon, A.M.,Godzik, A.,Lesley, S.A.,Sekimizu, K.,Wilson, I.A.
Structure of a virulence regulatory factor CvfB reveals a novel winged helix RNA binding module.
Structure, 18:537-547, 2010

PubMed 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.

PubMed: 20399190
DOI: 10.1016/j.str.2010.02.007

Experimental method

X-RAY DIFFRACTION (1.4 Å)