4krw

Novel re-arrangement of an RsmA/cSRa family protein to create a structurally distinct new RNA-binding family member

spinqualitylabelsall models 4krw, resolution 2.01Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4krw is a 1 chain structure with sequence from Pseudomonas aeruginosa UCBPP-PA14. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: IOD Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A0H2ZIZ8_PSEAB Publication Abstract from PubMed In bacteria, the highly conserved RsmA/CsrA family of RNA-binding proteins functions as global posttranscriptional regulators acting on mRNA translation and stability. Through phenotypic complementation of an rsmA mutant in Pseudomonas aeruginosa, we discovered a family member, termed RsmN. Elucidation of the RsmN crystal structure and that of the complex with a hairpin from the sRNA, RsmZ, reveals a uniquely inserted alpha helix, which redirects the polypeptide chain to form a distinctly different protein fold to the domain-swapped dimeric structure of RsmA homologs. The overall beta sheet structure required for RNA recognition is, however, preserved with compensatory sequence and structure differences, allowing the RsmN dimer to target binding motifs in both structured hairpin loops and flexible disordered RNAs. Phylogenetic analysis indicates that, although RsmN appears unique to P. aeruginosa, homologous proteins with the inserted alpha helix are more widespread and arose as a consequence of a gene duplication event. Structural Rearrangement in an RsmA/CsrA Ortholog of Pseudomonas aeruginosa Creates a Dimeric RNA-Binding Protein, RsmN.,Morris ER, Hall G, Li C, Heeb S, Kulkarni RV, Lovelock L, Silistre H, Messina M, Camara M, Emsley J, Williams P, Searle MS Structure. 2013 Aug 13. pii: S0969-2126(13)00257-8. doi:, 10.1016/j.str.2013.07.007. PMID:23954502 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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