2a6t

<table><tr><td colspan='2'>[[2a6t]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Cbs_356 Cbs 356]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A6T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2A6T FirstGlance]. <br>

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2a6t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a6t OCA], [https://pdbe.org/2a6t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2a6t RCSB], [https://www.ebi.ac.uk/pdbsum/2a6t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2a6t ProSAT]</span></td></tr>

[[https://www.uniprot.org/uniprot/DCP2_SCHPO DCP2_SCHPO]] Catalytic component of the decapping complex necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP. Decapping is the major pathway of mRNA degradation in yeast. It occurs through deadenylation, decapping and subsequent 5' to 3' exonucleolytic decay of the transcript body.<ref>PMID:15671491</ref>

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== Publication Abstract from PubMed ==

Decapping is a key step in both general and nonsense-mediated 5' --&gt; 3' mRNA-decay pathways. Removal of the cap structure is catalyzed by the Dcp1-Dcp2 complex. The crystal structure of a C-terminally truncated Schizosaccharomyces pombe Dcp2p reveals two distinct domains: an all-helical N-terminal domain and a C-terminal domain that is a classic Nudix fold. The C-terminal domain of both Saccharomyces cerevisiae and S. pombe Dcp2p proteins is sufficient for decapping activity, although the N-terminal domain can affect the efficiency of Dcp2p function. The binding of Dcp2p to Dcp1p is mediated by a conserved surface on its N-terminal domain, and the N-terminal domain is required for Dcp1p to stimulate Dcp2p activity. The flexible nature of the N-terminal domain relative to the C-terminal domain suggests that Dcp1p binding to Dcp2p may regulate Dcp2p activity through conformational changes of the two domains.

Crystal structure and functional analysis of Dcp2p from Schizosaccharomyces pombe.,She M, Decker CJ, Chen N, Tumati S, Parker R, Song H Nat Struct Mol Biol. 2006 Jan;13(1):63-70. Epub 2005 Dec 11. PMID:16341225<ref>PMID:16341225</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 2a6t" style="background-color:#fffaf0;"></div>

[[Category: Cbs 356]]

[[Category: Chen, N]]

[[Category: She, M]]

[[Category: Song, H]]

[[Category: Alpha/beta/alpha]]

[[Category: Rna binding protein]]