1q67

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[[Image:1q67.gif|left|200px]]
 
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{{Structure
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==Crystal structure of Dcp1p==
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|PDB= 1q67 |SIZE=350|CAPTION= <scene name='initialview01'>1q67</scene>, resolution 2.30&Aring;
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<StructureSection load='1q67' size='340' side='right'caption='[[1q67]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1q67]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q67 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Q67 FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
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|GENE= DCP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1q67 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q67 OCA], [https://pdbe.org/1q67 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1q67 RCSB], [https://www.ebi.ac.uk/pdbsum/1q67 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1q67 ProSAT]</span></td></tr>
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|DOMAIN=
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</table>
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|RELATEDENTRY=
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== Function ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1q67 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q67 OCA], [http://www.ebi.ac.uk/pdbsum/1q67 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1q67 RCSB]</span>
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[https://www.uniprot.org/uniprot/DCP1_YEAST DCP1_YEAST] 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. DCP1 is activated by the DEAD-box helicase DHH1 and destabilizes the eIF-4F cap-binding complex from the mRNA.<ref>PMID:8757137</ref> <ref>PMID:8816497</ref> <ref>PMID:9482745</ref> <ref>PMID:9482746</ref> <ref>PMID:10508173</ref> <ref>PMID:10101156</ref> <ref>PMID:10075882</ref> <ref>PMID:10564284</ref> <ref>PMID:10409716</ref> <ref>PMID:10944120</ref> <ref>PMID:11139489</ref> <ref>PMID:11741542</ref> <ref>PMID:12032091</ref> <ref>PMID:12054793</ref> <ref>PMID:12554866</ref> <ref>PMID:15024087</ref>
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}}
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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'''Crystal structure of Dcp1p'''
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/q6/1q67_consurf.spt"</scriptWhenChecked>
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==Overview==
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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A major pathway of eukaryotic mRNA turnover begins with deadenylation, followed by decapping and 5'--&gt;3' exonucleolytic degradation. A critical step in this pathway is decapping, which is carried out by an enzyme composed of Dcp1p and Dcp2p. The crystal structure of Dcp1p shows that it markedly resembles the EVH1 family of protein domains. Comparison of the proline-rich sequence (PRS)-binding sites in this family of proteins with Dcp1p indicates that it belongs to a novel class of EVH1 domains. Mapping of the sequence conservation on the molecular surface of Dcp1p reveals two prominent sites. One of these is required for the function of the Dcp1p-Dcp2p complex, and the other, corresponding to the PRS-binding site of EVH1 domains, is probably a binding site for decapping regulatory proteins. Moreover, a conserved hydrophobic patch is shown to be critical for decapping.
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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==About this Structure==
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1q67 ConSurf].
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1Q67 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q67 OCA].
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<div style="clear:both"></div>
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== References ==
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==Reference==
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<references/>
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Crystal structure of Dcp1p and its functional implications in mRNA decapping., She M, Decker CJ, Sundramurthy K, Liu Y, Chen N, Parker R, Song H, Nat Struct Mol Biol. 2004 Mar;11(3):249-56. Epub 2004 Feb 1. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14758354 14758354]
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Single protein]]
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[[Category: Chen N]]
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[[Category: Chen, N.]]
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[[Category: Decker CJ]]
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[[Category: Decker, C J.]]
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[[Category: Liu Y]]
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[[Category: Liu, Y.]]
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[[Category: Parker R]]
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[[Category: Parker, R.]]
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[[Category: She M]]
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[[Category: She, M.]]
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[[Category: Song H]]
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[[Category: Song, H.]]
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[[Category: beta sandwich]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:09:20 2008''
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Current revision

Crystal structure of Dcp1p

PDB ID 1q67

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