4clq
From Proteopedia
(Difference between revisions)
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- | ''' | + | ==Structure of Rcl1p - Bms1p complex== |
+ | <StructureSection load='4clq' size='340' side='right' caption='[[4clq]], [[Resolution|resolution]] 2.02Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[4clq]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CLQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CLQ FirstGlance]. <br> | ||
+ | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=4clq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4clq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4clq RCSB], [http://www.ebi.ac.uk/pdbsum/4clq PDBsum]</span></td></tr> | ||
+ | </table> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | The essential Rcl1p and Bms1p proteins form a complex required for 40S ribosomal subunit maturation. Bms1p is a GTPase and Rcl1p has been proposed to catalyse the endonucleolytic cleavage at site A2 separating the pre-40S and pre-60S maturation pathways. We determined the 2.0 A crystal structure of Bms1p associated with Rcl1p. We demonstrate that Rcl1p nuclear import depends on Bms1p and that the two proteins are loaded into pre-ribosomes at a similar stage of the maturation pathway and remain present within pre-ribosomes after cleavage at A2. Importantly, GTP binding to Bms1p is not required for the import in the nucleus nor for the incorporation of Rcl1p into pre-ribosomes, but is essential for early pre-rRNA processing. We propose that GTP binding to Bms1p and/or GTP hydrolysis may induce conformational rearrangements within the Bms1p-Rcl1p complex allowing the interaction of Rcl1p with its RNA substrate. | ||
- | + | Crucial role of the Rcl1p-Bms1p interaction for yeast pre-ribosomal RNA processing.,Delprato A, Al Kadri Y, Perebaskine N, Monfoulet C, Henry Y, Henras AK, Fribourg S Nucleic Acids Res. 2014;42(15):10161-72. doi: 10.1093/nar/gku682. Epub 2014 Jul, 26. PMID:25064857<ref>PMID:25064857</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | == References == | |
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Fribourg, S]] | ||
+ | [[Category: Translation]] |
Revision as of 07:59, 26 November 2014
Structure of Rcl1p - Bms1p complex
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