5cv1: Difference between revisions

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'''Unreleased structure'''


The entry 5cv1 is ON HOLD  until Paper Publication
==C. elegans PGL-1 Dimerization Domain==
<StructureSection load='5cv1' size='340' side='right'caption='[[5cv1]], [[Resolution|resolution]] 3.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5cv1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CV1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CV1 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.599&#8491;</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=5cv1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cv1 OCA], [https://pdbe.org/5cv1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cv1 RCSB], [https://www.ebi.ac.uk/pdbsum/5cv1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cv1 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PGL1_CAEEL PGL1_CAEEL] Essential role in male and female postembryonic germline development; maternally provided protein maintains a population of proliferating germ cells and zygotic expression is required for correct oogenesis. Predicted to bind RNA.<ref>PMID:9741628</ref>
<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.


Authors: Aoki, S.T., Bingman, C.A., Wickens, M., Kimble, J.E.
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>


Description: C. elegans PGL-1 Dimerization Domain
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Kimble, J.E]]
<div class="pdbe-citations 5cv1" style="background-color:#fffaf0;"></div>
[[Category: Bingman, C.A]]
== References ==
[[Category: Wickens, M]]
<references/>
[[Category: Aoki, S.T]]
__TOC__
</StructureSection>
[[Category: Caenorhabditis elegans]]
[[Category: Large Structures]]
[[Category: Aoki ST]]
[[Category: Bingman CA]]
[[Category: Kimble JE]]
[[Category: Wickens M]]
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