2bti: Difference between revisions

The RsmA family of RNA-binding proteins are global post-transcriptional, regulators that mediate extensive changes in gene expression in bacteria., They bind to, and affect the translation rate of target mRNAs, a function, that is further modulated by one or more, small, untranslated competitive, regulatory RNAs. To gain new insights into the nature of this protein/RNA, interaction, we used X-ray crystallography to solve the structure of the, Yersinia enterocolitica RsmA homologue. RsmA consists of a dimeric beta, barrel from which two alpha helices are projected. From structure-based, alignments of the RsmA protein family from diverse bacteria, we identified, key amino acid residues likely to be involved in RNA-binding., Site-specific mutagenesis revealed that arginine at position 44, located, at the N terminus of the alpha helix is essential for biological activity, in vivo and RNA-binding in vitro. Mutation of this site affects swarming, motility, exoenzyme and secondary metabolite production in the human, pathogen Pseudomonas aeruginosa, carbon metabolism in Escherichia coli, and hydrogen cyanide production in the plant beneficial strain Pseudomonas, fluorescens CHA0. R44A mutants are also unable to interact with the small, untranslated RNA, RsmZ. Thus, although possessing a motif similar to the, KH domain of some eukaryotic RNA-binding proteins, RsmA differs, substantially and incorporates a novel class of RNA-binding site.

2BTI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Yersinia_enterocolitica Yersinia enterocolitica] with SO4 and ACT as [http://en.wikipedia.org/wiki/ligands ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BTI OCA].  

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