PMID:15866937
| Citation |
Gutiérrez, P, Li, Y, Osborne, MJ, Pomerantseva, E, Liu, Q and Gehring, K (2005) Solution structure of the carbon storage regulator protein CsrA from Escherichia coli. J. Bacteriol. 187:3496-501 |
|---|---|
| Abstract |
The carbon storage regulator A (CsrA) is a protein responsible for the repression of a variety of stationary-phase genes in bacteria. In this work, we describe the nuclear magnetic resonance (NMR)-based structure of the CsrA dimer and its RNA-binding properties. CsrA is a dimer of two identical subunits, each composed of five strands, a small alpha-helix and a flexible C terminus. NMR titration experiments suggest that the beta1-beta2 and beta3-beta4 loops and the C-terminal helix are important elements in RNA binding. Even though the beta3-beta4 loop contains a highly conserved RNA-binding motif, GxxG, typical of KH domains, our structure excludes CsrA from being a member of this protein family, as previously suggested. A mechanism for the recognition of mRNAs downregulated by CsrA is proposed. |
| Links |
PubMed PMC1112004 Online version:10.1128/JB.187.10.3496-3501.2005 |
| Keywords |
Amino Acid Sequence; Carbon/metabolism; Dimerization; Electrochemistry; Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Molecular Sequence Data; Nuclear Magnetic Resonance, Biomolecular; Protein Structure, Tertiary; RNA, Messenger/physiology; RNA-Binding Proteins/chemistry; RNA-Binding Proteins/genetics; RNA-Binding Proteins/metabolism; Repressor Proteins/chemistry; Repressor Proteins/genetics; Repressor Proteins/metabolism |
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