5t9p

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'''Unreleased structure'''
 
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The entry 5t9p is ON HOLD until Paper Publication
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==Structural analysis reveals the flexible C-terminus of Nop15 undergoes rearrangement to recognize a pre-ribosomal RNA folding intermediate==
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<StructureSection load='5t9p' size='340' side='right' caption='[[5t9p]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5t9p]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5T9P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5T9P FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<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=5t9p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5t9p OCA], [http://pdbe.org/5t9p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5t9p RCSB], [http://www.ebi.ac.uk/pdbsum/5t9p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5t9p ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/NOP15_YEAST NOP15_YEAST]] Involved in the biogenesis of the 60S ribosomal subunit. Required for pre-rRNA processing and cytokinesis. Associates with the precursors of the 25S and 5.8S rRNAs.<ref>PMID:11583614</ref> <ref>PMID:14657029</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The RNA recognition motif (RRM) is the most abundant RNA-binding domain in eukaryotes, and it plays versatile roles in RNA metabolism. Despite its abundance, diversity of RRM structure and function is generated by variations on a conserved core. Yeast Nop15 is an RRM protein that is essential for large ribosomal subunit biogenesis. We determined a 2.0 A crystal structure of Nop15 that reveals a C-terminal alpha-helical region obscures its canonical RNA-binding surface. Small-angle X-ray scattering, NMR and RNA-binding analyses further reveal that the C-terminal residues of Nop15 are highly flexible, but essential for tight RNA binding. Moreover, comparison with a recently reported cryo-electron microscopy structure indicates that dramatic rearrangement of the C-terminal region of Nop15 in the pre-ribosome exposes the RNA-binding surface to recognize the base of its stem-loop target RNA and extends a newly-formed alpha helix to the distal loop where it forms protein interactions.
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Authors:
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Structural analysis reveals the flexible C-terminus of Nop15 undergoes rearrangement to recognize a pre-ribosomal RNA folding intermediate.,Zhang J, Gonzalez LE, Hall TM Nucleic Acids Res. 2016 Oct 26. pii: gkw961. PMID:27789691<ref>PMID:27789691</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 5t9p" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Gonzalez, E L]]
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[[Category: Hall, M T.T]]
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[[Category: Zhang, J]]
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[[Category: Nop15]]
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[[Category: Ribosomal protein]]
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[[Category: Rrm]]

Revision as of 03:30, 10 December 2016

Structural analysis reveals the flexible C-terminus of Nop15 undergoes rearrangement to recognize a pre-ribosomal RNA folding intermediate

5t9p, resolution 2.00Å

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