4qmf

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4qmf]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. 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 [https://proteopedia.org/fgij/fg.htm?mol=4QMF FirstGlance]. <br>
<table><tr><td colspan='2'>[[4qmf]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. 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 [https://proteopedia.org/fgij/fg.htm?mol=4QMF FirstGlance]. <br>
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</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=4qmf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qmf OCA], [https://pdbe.org/4qmf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qmf RCSB], [https://www.ebi.ac.uk/pdbsum/4qmf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qmf ProSAT]</span></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.804&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4qmf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qmf OCA], [https://pdbe.org/4qmf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qmf RCSB], [https://www.ebi.ac.uk/pdbsum/4qmf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qmf ProSAT]</span></td></tr>
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</table>
== Function ==
== Function ==
[https://www.uniprot.org/uniprot/KRR1_YEAST KRR1_YEAST] Required for 40S ribosome biogenesis. Involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly. Essential for vegetative growth.<ref>PMID:11996121</ref> <ref>PMID:11027267</ref> <ref>PMID:15094838</ref> <ref>PMID:15590835</ref>
[https://www.uniprot.org/uniprot/KRR1_YEAST KRR1_YEAST] Required for 40S ribosome biogenesis. Involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly. Essential for vegetative growth.<ref>PMID:11996121</ref> <ref>PMID:11027267</ref> <ref>PMID:15094838</ref> <ref>PMID:15590835</ref>
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== Publication Abstract from PubMed ==
 
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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.
 
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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>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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<div class="pdbe-citations 4qmf" style="background-color:#fffaf0;"></div>
 
== References ==
== References ==
<references/>
<references/>

Current revision

Structure of the Krr1 and Faf1 complex from Saccharomyces cerevisiae

PDB ID 4qmf

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