4qmf: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4qmf]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QMF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QMF FirstGlance]. <br> | <table><tr><td colspan='2'>[[4qmf]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QMF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QMF FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4qmf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qmf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4qmf RCSB], [http://www.ebi.ac.uk/pdbsum/4qmf PDBsum]</span></td></tr> | </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=4qmf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qmf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4qmf RCSB], [http://www.ebi.ac.uk/pdbsum/4qmf PDBsum]</span></td></tr> | ||
<table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Ribosome formation in Saccharomyces cerevisiae requires a large number of transiently associated assembly factors that coordinate processing and folding of pre-rRNA and binding of ribosomal proteins. Krr1 and Faf1 are two interacting proteins present in early 90 S precursor particles of the small ribosomal subunit. Here, we determined a co-crystal structure of the core domain of Krr1 bound to a 19-residue fragment of Faf1 at 2.8 A resolution. The structure reveals that Krr1 consists of two packed K homology (KH) domains, KH1 and KH2, and resembles archaeal Dim2-like proteins. We show that KH1 is a divergent KH domain that lacks the RNA-binding GXXG motif and is involved in binding another assembly factor, Kri1. KH2 contains a canonical RNA-binding surface and additionally associates with an alpha-helix of Faf1. Specific disruption of the Krr1-Faf1 interaction impaired early 18 S rRNA processing at sites A0, A1, and A2 and caused cell lethality, but it did not prevent incorporation of the two proteins into pre-ribosomes. The Krr1-Faf1 interaction likely maintains a critical conformation of 90 S pre-ribosomes required for pre-rRNA processing. Our results illustrate the versatility of KH domains in protein interaction and provide insight into the role of Krr1-Faf1 interaction in ribosome biogenesis. | |||
Interaction between ribosome assembly factors Krr1 and Faf1 is essential for formation of small ribosomal subunit in yeast.,Zheng S, Lan P, Liu X, Ye K J Biol Chem. 2014 Aug 15;289(33):22692-703. doi: 10.1074/jbc.M114.584490. Epub, 2014 Jul 2. PMID:24990943<ref>PMID:24990943</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Ye, K | [[Category: Ye, K]] | ||
[[Category: Zheng, S | [[Category: Zheng, S]] | ||
[[Category: K-homology domain]] | [[Category: K-homology domain]] | ||
[[Category: Protein-protein complex]] | [[Category: Protein-protein complex]] | ||
[[Category: Ribosome biogenesis]] | [[Category: Ribosome biogenesis]] | ||
[[Category: Rna binding protein]] | [[Category: Rna binding protein]] | ||
Revision as of 12:29, 10 December 2014
Structure of the Krr1 and Faf1 complex from Saccharomyces cerevisiae
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