View source for 5lsl


==Crystal structure of yeast Hsh49p in complex with Cus1p binding domain.==
<StructureSection load='5lsl' size='340' side='right'caption='[[5lsl]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5lsl]] is a 8 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=5LSL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LSL FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.65&#8491;</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=5lsl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lsl OCA], [https://pdbe.org/5lsl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lsl RCSB], [https://www.ebi.ac.uk/pdbsum/5lsl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lsl ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/HSH49_YEAST HSH49_YEAST] Possible SF3b-like factor.
<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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5lsl" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Nagai K]]
[[Category: Obayashi E]]
[[Category: Oubridge C]]
[[Category: Sposito B]]
[[Category: Van Roon AM]]