2e5g
From Proteopedia
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- | [[Image:2e5g.png|left|200px]] | ||
- | + | ==Solution structure of RNA binding domain in RNA binding motif protein 21== | |
+ | <StructureSection load='2e5g' size='340' side='right'caption='[[2e5g]]' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[2e5g]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2E5G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2E5G FirstGlance]. <br> | ||
+ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2e5g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e5g OCA], [https://pdbe.org/2e5g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2e5g RCSB], [https://www.ebi.ac.uk/pdbsum/2e5g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2e5g ProSAT], [https://www.topsan.org/Proteins/RSGI/2e5g TOPSAN]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/STPAP_HUMAN STPAP_HUMAN] Poly(A) polymerase that creates the 3'-poly(A) tail of specific pre-mRNAs. Localizes to nuclear speckles together with PIP5K1A and mediates polyadenylation of a select set of mRNAs, such as HMOX1. In addition to polyadenylation, it is also required for the 3'-end cleavage of pre-mRNAs: binds to the 3'UTR of targeted pre-mRNAs and promotes the recruitment and assembly of the CPSF complex on the 3'UTR of pre-mRNAs. In addition to adenylyltransferase activity, also has uridylyltransferase activity. However, the ATP ratio is higher than UTP in cells, suggesting that it functions primarily as a poly(A) polymerase. Acts as a specific terminal uridylyltransferase for U6 snRNA in vitro: responsible for a controlled elongation reaction that results in the restoration of the four 3'-terminal UMP-residues found in newly transcribed U6 snRNA. Not involved in replication-dependent histone mRNA degradation.<ref>PMID:16790842</ref> <ref>PMID:18288197</ref> <ref>PMID:21102410</ref> | ||
+ | == Evolutionary Conservation == | ||
+ | [[Image:Consurf_key_small.gif|200px|right]] | ||
+ | Check<jmol> | ||
+ | <jmolCheckbox> | ||
+ | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e5/2e5g_consurf.spt"</scriptWhenChecked> | ||
+ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
+ | <text>to colour the structure by Evolutionary Conservation</text> | ||
+ | </jmolCheckbox> | ||
+ | </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=2e5g ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
- | === | + | ==See Also== |
- | + | *[[RNA uridylyltransferase|RNA uridylyltransferase]] | |
- | + | == References == | |
- | == | + | <references/> |
- | + | __TOC__ | |
+ | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
- | [[Category: | + | [[Category: Large Structures]] |
- | [[Category: Inoue | + | [[Category: Inoue M]] |
- | [[Category: Kigawa | + | [[Category: Kigawa T]] |
- | [[Category: Muto | + | [[Category: Muto Y]] |
- | + | [[Category: Shirouzu M]] | |
- | [[Category: Shirouzu | + | [[Category: Terada T]] |
- | [[Category: Terada | + | [[Category: Tsuda K]] |
- | [[Category: Tsuda | + | [[Category: Yokoyama S]] |
- | [[Category: Yokoyama | + | |
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Current revision
Solution structure of RNA binding domain in RNA binding motif protein 21
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Categories: Homo sapiens | Large Structures | Inoue M | Kigawa T | Muto Y | Shirouzu M | Terada T | Tsuda K | Yokoyama S