2x1b: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
No edit summary
OCA (talk | contribs)
No edit summary
 
(8 intermediate revisions by the same user not shown)
Line 1: Line 1:
{{Seed}}
[[Image:2x1b.png|left|200px]]


<!--
==Structure of RNA15 RRM==
The line below this paragraph, containing "STRUCTURE_2x1b", creates the "Structure Box" on the page.
<StructureSection load='2x1b' size='340' side='right'caption='[[2x1b]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[2x1b]] is a 1 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=2X1B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2X1B FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
-->
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
{{STRUCTURE_2x1b|  PDB=2x1b  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2x1b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x1b OCA], [https://pdbe.org/2x1b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2x1b RCSB], [https://www.ebi.ac.uk/pdbsum/2x1b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2x1b ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RNA15_YEAST RNA15_YEAST] RNA-binding component of the cleavage factor IA (CFIA) complex, which is involved in the endonucleolytic cleavage during polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with the cleavage factor NAB4/CFIB and the cleavage and polyadenylation factor (CPF) complex. Binds to A-rich RNA sequence elements.<ref>PMID:7992054</ref> <ref>PMID:11344258</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/x1/2x1b_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=2x1b ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Rna15 is a core subunit of cleavage factor IA (CFIA), an essential transcriptional 3'-end processing factor from Saccharomyces cerevisiae. CFIA is required for polyA site selection/cleavage targeting RNA sequences that surround polyadenylation sites in the 3'-UTR of RNA polymerase-II transcripts. RNA recognition by CFIA is mediated by an RNA recognition motif (RRM) contained in the Rna15 subunit of the complex. We show here that Rna15 has a strong and unexpected preference for GU containing RNAs and reveal the molecular basis for a base selectivity mechanism that accommodates G or U but discriminates against C and A bases. This mode of base selectivity is rather different to that observed in other RRM-RNA structures and is structurally conserved in CstF64, the mammalian counterpart of Rna15. Our observations provide evidence for a highly conserved mechanism of base recognition amongst the 3'-end processing complexes that interact with the U-rich or U/G-rich elements at 3'-end cleavage/polyadenylation sites.


===STRUCTURE OF RNA15 RRM===
Structure of the Rna15 RRM-RNA complex reveals the molecular basis of GU specificity in transcriptional 3'-end processing factors.,Pancevac C, Goldstone DC, Ramos A, Taylor IA Nucleic Acids Res. 2010 May;38(9):3119-32. Epub 2010 Jan 21. PMID:20097654<ref>PMID:20097654</ref>


 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
<!--
</div>
The line below this paragraph, {{ABSTRACT_PUBMED_20097654}}, adds the Publication Abstract to the page
<div class="pdbe-citations 2x1b" style="background-color:#fffaf0;"></div>
(as it appears on PubMed at http://www.pubmed.gov), where 20097654 is the PubMed ID number.
== References ==
-->
<references/>
{{ABSTRACT_PUBMED_20097654}}
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Large Structures]]
2X1B is a 1 chain structure with 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=2X1B OCA].
 
==Reference==
<ref group="xtra">PMID:20097654</ref><references group="xtra"/>
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Goldstone, D C.]]
[[Category: Goldstone DC]]
[[Category: Pancevac, C.]]
[[Category: Pancevac C]]
[[Category: Ramos, A.]]
[[Category: Ramos A]]
[[Category: Taylor, I A.]]
[[Category: Taylor IA]]
[[Category: Mrna processing]]
[[Category: Nucleus]]
[[Category: Rna-binding]]
[[Category: Transcription]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May 26 08:37:40 2010''

Latest revision as of 10:19, 9 May 2024

Structure of RNA15 RRM

2x1b, resolution 1.80Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA