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2jpp

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2jpp

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Structural basis of RsmA/CsrA RNA recognition: Structure of RsmE bound to the Shine-Dalgarno sequence of hcnA mRNA

Overview

Proteins of the RsmA/CsrA family are global translational regulators in, many bacterial species. We have determined the solution structure of a, complex formed between the RsmE protein, a member of this family from, Pseudomonas fluorescens, and a target RNA encompassing the, ribosome-binding site of the hcnA gene. The RsmE homodimer with its two, RNA-binding sites makes optimal contact with an, 5'-(A)/(U)CANGGANG(U)/(A)-3' sequence in the mRNA. When tightly gripped by, RsmE, the ANGGAN core folds into a loop, favoring the formation of a, 3-base-pair stem by flanking nucleotides. We validated these findings by, in vivo and in vitro mutational analyses. The structure of the complex, explains well how, by sequestering the Shine-Dalgarno sequence, the, RsmA/CsrA proteins repress translation.

About this Structure

2JPP is a Single protein structure of sequence from Pseudomonas fluorescens. Full crystallographic information is available from OCA.

Reference

Molecular basis of messenger RNA recognition by the specific bacterial repressing clamp RsmA/CsrA., Schubert M, Lapouge K, Duss O, Oberstrass FC, Jelesarov I, Haas D, Allain FH, Nat Struct Mol Biol. 2007 Sep;14(9):807-13. Epub 2007 Aug 19. PMID:17704818

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