5mpx | pdb_00005mpx

Crystal structure of Arabidopsis thaliana RNA editing factor MORF1, space group P2(1)

spinqualitylabelsall models 5mpx, resolution 1.94Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5mpx is a 4 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.938Å Ligands: SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function MORF1_ARATH Involved in organellar RNA editing. Required for the processing of numerous RNA editing sites in mitochondria (PubMed:22411807, PubMed:23818871). Binds to the mitochondrial MEF19 and MEF21 factors, two pentatricopeptide repeat-containing proteins involved in RNA editing (PubMed:22411807). Publication Abstract from PubMed In flowering plant plastids and mitochondria, multiple organellar RNA editing factor (MORF/RIP) proteins are required at most sites for efficient C to U RNA editing catalyzed by the RNA editosome. MORF proteins harbor a conserved stretch of residues (MORF-box), form homo- and heteromers and interact with selected PPR (pentatricopeptide repeat) proteins, which recognize each editing site. The molecular function of the MORF-box remains elusive since it shares no sequence similarity with known domains. We determined structures of the A. thaliana mitochondrial MORF1 and chloroplast MORF9 MORF-boxes which both adopt a novel globular fold (MORF domain). Our structures state a paradigmatic model for MORF domains and their specific dimerization via a hydrophobic interface. We cross-validate the interface by yeast two-hybrid studies and pulldown assays employing structure-based mutants. We find a structural similarity of the MORF domain to an N-terminal ferredoxin-like domain (NFLD), which confers RNA substrate positioning in bacterial 4-thio-uracil tRNA synthetases, implying direct RNA contacts of MORF proteins during RNA editing. With the MORF1 and MORF9 structures we elucidate a yet unknown fold, corroborate MORF interaction studies, validate the mechanism of MORF multimerization by structure-based mutants and pave the way towards a complete structural characterization of the plant RNA editosome. Crystal structures of the Arabidopsis thaliana organellar RNA editing factors MORF1 and MORF9.,Haag S, Schindler M, Berndt L, Brennicke A, Takenaka M, Weber G Nucleic Acids Res. 2017 May 5;45(8):4915-4928. doi: 10.1093/nar/gkx099. PMID:28201607 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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