1Y00

Solution structure of the Carbon Storage Regulator protein CsrA

Summary for 1Y00

• Entry DOI: 10.2210/pdb1y00/pdb
• NMR Information: BMRB: 6402
• Descriptor: Carbon storage regulator (1 entity in total)
• Functional Keywords: carbon storage regulation, montreal-kingston bacterial structural genomics initiative, bsgi, structural genomics, rna binding protein
• Biological source: Escherichia coli
• Total number of polymer chains: 2
• Total formula weight: 13729.76

Authors

Gutierrez, P.,Li, Y.,Osborne, M.J.,Liu, Q.,Gehring, K.,Montreal-Kingston Bacterial Structural Genomics Initiative (BSGI) (deposition date: 2004-11-13, release date: 2005-06-21, Last modification date: 2024-05-22)

Primary citation

Gutierrez, P.,Li, Y.,Osborne, M.J.,Pomerantseva, E.,Liu, Q.,Gehring, K.
Solution structure of the carbon storage regulator protein CsrA from Escherichia coli.
J.Bacteriol., 187:3496-3501, 2005

PubMed 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.

PubMed: 15866937
DOI: 10.1128/JB.187.10.3496-3501.2005

Experimental method

SOLUTION NMR