2JPP

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

Summary for 2JPP

• Entry DOI: 10.2210/pdb2jpp/pdb
• NMR Information: BMRB: 15257
• Descriptor: RNA (5'-R(*GP*GP*GP*CP*UP*UP*CP*AP*CP*GP*GP*AP*UP*GP*AP*AP*GP*CP*CP*C)-3'), Translational repressor (2 entities in total)
• Functional Keywords: rna recognition, protein/rna, csra, rsma, shine-dalgarno, translation-rna complex, translation/rna
• Biological source: Pseudomonas fluorescens
• Total number of polymer chains: 4
• Total formula weight: 28571.69

Authors

Schubert, M.,Lapouge, K.,Duss, O.,Oberstrass, F.C.,Jelesarov, I.,Haas, D.,Allain, F.H.-T. (deposition date: 2007-05-21, release date: 2007-08-21, Last modification date: 2023-12-20)

Primary citation

Schubert, M.,Lapouge, K.,Duss, O.,Oberstrass, F.C.,Jelesarov, I.,Haas, D.,Allain, F.H.-T.
Molecular basis of messenger RNA recognition by the specific bacterial repressing clamp RsmA/CsrA
Nat.Struct.Mol.Biol., 14:807-813, 2007

PubMed Abstract: 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/UCANGGANGU/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.

PubMed: 17704818
DOI: 10.1038/nsmb1285

Experimental method

SOLUTION NMR