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5cv3
From Proteopedia
(Difference between revisions)
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| - | ''' | + | ==C. remanei PGL-1 Dimerization Domain - Hg== |
| + | <StructureSection load='5cv3' size='340' side='right' caption='[[5cv3]], [[Resolution|resolution]] 3.17Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5cv3]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CV3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CV3 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EMC:ETHYL+MERCURY+ION'>EMC</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5cow|5cow]]</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=5cv3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cv3 OCA], [http://pdbe.org/5cv3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5cv3 RCSB], [http://www.ebi.ac.uk/pdbsum/5cv3 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Cellular RNA-protein (RNP) granules are ubiquitous and have fundamental roles in biology and RNA metabolism, but the molecular basis of their structure, assembly, and function is poorly understood. Using nematode "P-granules" as a paradigm, we focus on the PGL granule scaffold protein to gain molecular insights into RNP granule structure and assembly. We first identify a PGL dimerization domain (DD) and determine its crystal structure. PGL-1 DD has a novel 13 alpha-helix fold that creates a positively charged channel as a homodimer. We investigate its capacity to bind RNA and discover unexpectedly that PGL-1 DD is a guanosine-specific, single-stranded endonuclease. Discovery of the PGL homodimer, together with previous results, suggests a model in which the PGL DD dimer forms a fundamental building block for P-granule assembly. Discovery of the PGL RNase activity expands the role of RNP granule assembly proteins to include enzymatic activity in addition to their job as structural scaffolds. | ||
| - | + | PGL germ granule assembly protein is a base-specific, single-stranded RNase.,Aoki ST, Kershner AM, Bingman CA, Wickens M, Kimble J Proc Natl Acad Sci U S A. 2016 Jan 19. pii: 201524400. PMID:26787882<ref>PMID:26787882</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 5cv3" style="background-color:#fffaf0;"></div> | |
| - | [[Category: | + | == References == |
| - | [[Category: Bingman, C | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Aoki, S T]] | ||
| + | [[Category: Bingman, C A]] | ||
| + | [[Category: Kimble, J E]] | ||
[[Category: Wickens, M]] | [[Category: Wickens, M]] | ||
| - | [[Category: | + | [[Category: Dimer]] |
| - | [[Category: | + | [[Category: Guanosine endonuclease]] |
| + | [[Category: Hydrolase]] | ||
| + | [[Category: P-granule]] | ||
Revision as of 15:41, 3 February 2016
C. remanei PGL-1 Dimerization Domain - Hg
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