5dcv

Crystal structure of PhoRpp38-SL12M complex

spinqualitylabelsall models 5dcv, resolution 3.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5dcv is a 4 chain structure with sequence from Pyrococcus horikoshii OT3. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.401Å Ligands: GTP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function RL7A_PYRHO Multifunctional RNA-binding protein that recognizes the K-turn motif in ribosomal RNA, box H/ACA, box C/D and box C'/D' sRNAs (By similarity). When added to reconstituted ribonuclease P (RNase P) it increases the optimum temperature to that of the partially purified enzyme and causes a 5-fold increase in apparent Vmax. Binds the RNase P catalytic RNA. Publication Abstract from PubMed PhoRpp38 in the hyperthermophilic archaeon Pyrococcus horikoshii, a homologue of human ribonuclease P (RNase P) protein Rpp38, belongs to the ribosomal protein L7Ae family that specifically recognizes a kink-turn (K-turn) motif. A previous biochemical study showed that PhoRpp38 specifically binds to two stem-loops, SL12 and SL16, containing helices P12.1/12.2 and P15/16 respectively, in P. horikoshii RNase P RNA (PhopRNA). In order to gain insight into the PhoRpp38 binding mode to PhopRNA, we determined the crystal structure of PhoRpp38 in complex with the SL12 mutant (SL12M) at a resolution of 3.4 A. The structure revealed that Lys35 on the beta-strand (beta1) and Asn38, Glu39, and Lys42 on the alpha-helix (alpha2) in PhoRpp38 interact with characteristic G*A and A*G pairs in SL12M, where Ile93, Glu94, and Val95, on a loop between alpha4 and beta4 in PhoRpp38, interact with the 3-nucleotide bulge (G-G-U) in the SL12M. The structure demonstrates the previously proposed secondary structure of SL12, including helix P12.2. Structure-based mutational analysis indicated that amino acid residues involved in the binding to SL12 are also responsible for the binding to SL16. This result suggested that each PhoRpp38 binds to the K-turns in SL12 and SL16 in PhopRNA. A pull-down assay further suggested the presence of a second K-turn in SL12. Based on the present results, together with available data, we discuss a structural basis for recognition of K-turn motifs in PhopRNA by PhoRpp38. Structural basis for recognition of a kink-turn motif by an archaeal homologue of human RNase P protein Rpp38.,Oshima K, Kakiuchi Y, Tanaka Y, Ueda T, Nakashima T, Kimura M, Yao M Biochem Biophys Res Commun. 2016 Jun 3;474(3):541-6. doi:, 10.1016/j.bbrc.2016.04.118. Epub 2016 Apr 23. PMID:27114305 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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