5eip

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==apo-structure of YTH domain of SpMmi1==
==apo-structure of YTH domain of SpMmi1==
<StructureSection load='5eip' size='340' side='right' caption='[[5eip]], [[Resolution|resolution]] 1.49&Aring;' scene=''>
<StructureSection load='5eip' size='340' side='right' caption='[[5eip]], [[Resolution|resolution]] 1.49&Aring;' scene=''>
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<table><tr><td colspan='2'>[[5eip]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EIP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5EIP FirstGlance]. <br>
<table><tr><td colspan='2'>[[5eip]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EIP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5EIP FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5eim|5eim]]</td></tr>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5eim|5eim]]</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5eip FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5eip OCA], [http://pdbe.org/5eip PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5eip RCSB], [http://www.ebi.ac.uk/pdbsum/5eip PDBsum]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5eip FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5eip OCA], [http://pdbe.org/5eip PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5eip RCSB], [http://www.ebi.ac.uk/pdbsum/5eip PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5eip ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/MMI1_SCHPO 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]<ref>PMID:16823445</ref>
[[http://www.uniprot.org/uniprot/MMI1_SCHPO 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]<ref>PMID:16823445</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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<ref>PMID:28735863</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5eip" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>

Revision as of 04:36, 21 September 2017

apo-structure of YTH domain of SpMmi1

5eip, resolution 1.49Å

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