1y00
From Proteopedia
Solution structure of the Carbon Storage Regulator protein CsrA
Structural highlights
Function[CSRA_ECOLI] Binds to mRNA to regulate post-transcriptional activity. Affects glycogen biosynthesis, gluconeogenesis, cell size and surface properties. Regulates glycogen synthesis under both aerobic and anaerobic conditions. Seems to accelerate the degradation of glg gene transcripts, potentially through selective RNA binding. Acts to inhibit interaction between the LetD protein and the A subunit of DNA gyrase. Also required for motility and flagellum biosynthesis through the post-transcriptional activation of flhDC expression. This involves binding to and stabilization of the flhDC message by CsrA. Binds to and reduces levels of probable diguanylate cyclases ycdT and ydeH.[1] [2] [3] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. Solution structure of the carbon storage regulator protein CsrA from Escherichia coli.,Gutierrez P, Li Y, Osborne MJ, Pomerantseva E, Liu Q, Gehring K J Bacteriol. 2005 May;187(10):3496-501. PMID:15866937[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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