5lsb: Difference between revisions

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'''Unreleased structure'''


The entry 5lsb is ON HOLD  until Paper Publication
==Crystal structure of yeast Hsh49p in complex with Cus1p binding domain.==
<StructureSection load='5lsb' size='340' side='right' caption='[[5lsb]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5lsb]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LSB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LSB FirstGlance]. <br>
</td></tr><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=5lsb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lsb OCA], [http://pdbe.org/5lsb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lsb RCSB], [http://www.ebi.ac.uk/pdbsum/5lsb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lsb ProSAT]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/HSH49_YEAST HSH49_YEAST]] Possible SF3b-like factor. [[http://www.uniprot.org/uniprot/CUS1_YEAST CUS1_YEAST]] Essential splicing protein required for U2 snRNP binding to pre-mRNA during spliceosome assembly.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Spliceosomal proteins Hsh49p and Cus1p are components of SF3b, which together with SF3a, Msl1p/Lea1p, Sm proteins and U2 snRNA, form U2 snRNP, which plays a crucial role in pre-mRNA splicing. Hsh49p, comprising two RRMs, forms a heterodimer with Cus1p. We determined the crystal structures of Saccharomyces cerevisiae full-length Hsh49p as well as its RRM1 in complex with a minimal binding region of Cus1p (residues 290-368). The structures show that the Cus1 fragment binds to the alpha-helical surface of Hsh49p RRM1, opposite the four-stranded beta-sheet, leaving the canonical RNA binding surface available to bind RNA. Hsh49p binds the 5' end region of U2 snRNA via RRM1. Its affinity is increased in complex with Cus1(290-368)p, partly because an extended RNA-binding surface forms across the protein-protein interface. The Hsh49p RRM1-Cus1(290-368)p structure fits well into cryo-EM density of the Bact spliceosome, corroborating the biological relevance of our crystal structure.


Authors:  
Crystal structure of U2 snRNP SF3b components: Hsh49p in complex with Cus1p binding domain.,van Roon AA, Oubridge C, Obayashi E, Sposito B, Newman AJ, Seraphin B, Nagai K RNA. 2017 Mar 27. pii: rna.059378.116. doi: 10.1261/rna.059378.116. PMID:28348170<ref>PMID:28348170</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 5lsb" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Nagai, K]]
[[Category: Obayashi, E]]
[[Category: Oubridge, C]]
[[Category: Roon, A M.van]]
[[Category: Sposito, B]]
[[Category: Rna binding domain]]
[[Category: Sf3b complex]]
[[Category: Splicing]]
[[Category: U2 snrnp]]
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