5cv3
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5cv3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Caenorhabditis_remanei Caenorhabditis remanei]. 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 [https://proteopedia.org/fgij/fg.htm?mol=5CV3 FirstGlance]. <br> | <table><tr><td colspan='2'>[[5cv3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Caenorhabditis_remanei Caenorhabditis remanei]. 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 [https://proteopedia.org/fgij/fg.htm?mol=5CV3 FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EMC:ETHYL+MERCURY+ION'>EMC</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.1701477Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EMC:ETHYL+MERCURY+ION'>EMC</scene></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=5cv3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cv3 OCA], [https://pdbe.org/5cv3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cv3 RCSB], [https://www.ebi.ac.uk/pdbsum/5cv3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cv3 ProSAT]</span></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=5cv3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cv3 OCA], [https://pdbe.org/5cv3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cv3 RCSB], [https://www.ebi.ac.uk/pdbsum/5cv3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cv3 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/PGL1_CAERE PGL1_CAERE] Guanyl-specific endoribonuclease which cleaves the phosphodiester bond in single-stranded RNA between the 3'-guanylic residue and the 5'-OH residue of adjacent nucleotide, resulting in the formation of a corresponding 2',3'-cyclic phosphate intermediate (PubMed:26787882). 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 (By similarity). Together with the P-granule component pgl-3, is involved in the formation of P-granules (By similarity). Together with pgl-3, probably recruits other granule components such as pos-1, mex-3 and glh-1 to P-granules (By similarity). In addition, may act redundantly with pgl-3 to protect germ cells from excessive germline apoptosis during normal oogenesis and development of the two gonadal arms (By similarity). This may in part be through regulating the localization of sir-2.1 which is involved in germ cell apoptosis (By similarity). May protect somatic cells from excessive apoptosis during normal development (By similarity).[UniProtKB:Q9TZQ3]<ref>PMID:26787882</ref> | [https://www.uniprot.org/uniprot/PGL1_CAERE PGL1_CAERE] Guanyl-specific endoribonuclease which cleaves the phosphodiester bond in single-stranded RNA between the 3'-guanylic residue and the 5'-OH residue of adjacent nucleotide, resulting in the formation of a corresponding 2',3'-cyclic phosphate intermediate (PubMed:26787882). 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 (By similarity). Together with the P-granule component pgl-3, is involved in the formation of P-granules (By similarity). Together with pgl-3, probably recruits other granule components such as pos-1, mex-3 and glh-1 to P-granules (By similarity). In addition, may act redundantly with pgl-3 to protect germ cells from excessive germline apoptosis during normal oogenesis and development of the two gonadal arms (By similarity). This may in part be through regulating the localization of sir-2.1 which is involved in germ cell apoptosis (By similarity). May protect somatic cells from excessive apoptosis during normal development (By similarity).[UniProtKB:Q9TZQ3]<ref>PMID:26787882</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. | ||
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| - | 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> | ||
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| - | 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> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Current revision
C. remanei PGL-1 Dimerization Domain - Hg
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