5eim | pdb_00005eim

YTH domain-containing protein mmi1 and RNA complex

spinqualitylabelsall models 5eim, resolution 1.54Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5eim is a 4 chain structure with sequence from Schizosaccharomyces pombe 972h- and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.54Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function MMI1_SCHPO RNA-binding protein that recognizes and binds N6-methyladenosine (m6A)-containing RNAs, a modification present at internal sites of mRNAs and some non-coding RNAs (By similarity). Required for elemination of certain meiosis-specific mRNAs in an early event following transcription. May bind to the cis-acting region (DSR) of the mRNA, activating the nuclear exosome which may lead to the degradation of the transcript from the 3' region (PubMed:16823445).[UniProtKB:Q06390] Publication Abstract from PubMed Meiosis is one of the most dramatic differentiation programs accompanied by a striking change in gene expression profiles in fission yeast Schizosaccharomyces pombe. Whereas a number of meiosis-specific transcripts are expressed untimely in mitotic cells, and the entry of meiosis will be blocked as the accumulation of meiosis-specific mRNAs in the mitotic cells. A YTH domain containing protein Mmi1 was identified as a pivotal effector in a post-transcriptional event termed selective elimination of meiosis-specific mRNAs. Mmi1 can recognize and bind a class of meiosis-specific transcripts expressed inappropriately in mitotic cells, which all contain a conservative region called DSR, as a mark to remove them in cooperation with nuclear exosomes. Here we report the 1.6 A resolution crystal structure of the Mmi1-YTH domain in complex with a high consensus hexanucleotide motif, which is multiple copied in the DSR region. Our structure observations, supported by site-directed mutations of key residues illustrate the mechanism for specific recognition of DSR-RNA by Mmi1. Moreover, different from other YTH domain family proteins, Mmi1-YTH domain has a distinctive RNA-binding properties although it has a similar fold as other ones. Structural insights into the specific recognition of DSR by the YTH domain containing protein Mmi1.,Wu B, Xu J, Su S, Liu H, Gan J, Ma J Biochem Biophys Res Commun. 2017 Sep 16;491(2):310-316. doi:, 10.1016/j.bbrc.2017.07.104. Epub 2017 Jul 20. PMID:28735863 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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