PDBsum entry 2jpp

Translation/RNA

PDB id: 2jpp

Contents

Protein chains

53 a.a. *

DNA/RNA

* Residue conservation analysis

PDB id:

2jpp

Name:

Translation/RNA

Title:

Structural basis of rsma/csra RNA recognition: structure of rsme bound to the shine-dalgarno sequence of hcna mRNA

Structure:

RNA (5'- r( Gp Gp Gp Cp Up Up Cp Ap Cp Gp Gp Ap Up Gp Ap Ap Gp Cp Cp C)-3'). Chain: c, d. Engineered: yes. Translational repressor. Chain: a, b. Engineered: yes

Source:

Synthetic: yes. Pseudomonas fluorescens. Organism_taxid: 294. Gene: rsme. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

10 models

Authors:

M.Schubert,K.Lapouge,O.Duss,F.C.Oberstrass,I.Jelesarov,D.Haas,F.H.- T.Allain

Key ref:

M.Schubert et al. (2007). Molecular basis of messenger RNA recognition by the specific bacterial repressing clamp RsmA/CsrA. Nat Struct Biol, 14, 807-813. PubMed id: 17704818 DOI: 10.1038/nsmb1285

Date:

21-May-07 Release date: 21-Aug-07

Protein chains

P0DPC3  (CSRA1_PSEPH) -  Translational regulator CsrA1 from Pseudomonas protegens (strain DSM 19095 / LMG 27888 / CFBP 6595 / CHA0)

Seq: 64 a.a.

Struc: 53 a.a.

DNA/RNA chains

G-G-G-C-U-U-C-A-C-G-G-A-U-G-A-A-G-C-C-C 20 bases

G-G-G-C-U-U-C-A-C-G-G-A-U-G-A-A-G-C-C-C 20 bases

DOI no: 10.1038/nsmb1285

Nat Struct Biol 14:807-813 (2007)

PubMed id: 17704818

Molecular basis of messenger RNA recognition by the specific bacterial repressing clamp RsmA/CsrA.

M.Schubert, K.Lapouge, O.Duss, F.C.Oberstrass, I.Jelesarov, D.Haas, F.H.Allain.

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)/(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.

Selected figure(s)

Figure 2.
(a) Solution structure of the 2:2 complex of RsmE with 20-nucleotide hcnA sequence. Protein ribbons for each monomer are shown in green and gray. Heavy atoms of the two RNAs are shown in yellow and red. An orange ribbon linking the phosphates is also shown. (b) Surface representation of the RsmE dimer in complex, colored by electrostatic potential (blue, positive; red, negative). (c) Stereo view of one 20-nucleotide hcnA sequence bound to the edge of the RsmE dimer sandwich, omitting the second RNA molecule in the background; a representative structure is shown.

Figure 3.
(a–d) Structural details of interactions important for recognition. Black and green, side chains and backbone of RsmE monomers A and B, respectively; magenta dashed lines, possible hydrogen bonds. (e) Schematic representation of intermolecular RNA-protein interactions, colored as in a–d. Cyan, hydrophobic interactions.

The above figures are reprinted by permission from Macmillan Publishers Ltd: Nat Struct Biol (2007, 14, 807-813) copyright 2007.

Figures were selected by an automated process.