5CV3

C. remanei PGL-1 Dimerization Domain - Hg

Summary for 5CV3

• Entry DOI: 10.2210/pdb5cv3/pdb
• Related: 5COW
• Descriptor: Putative uncharacterized protein, ETHYL MERCURY ION (2 entities in total)
• Functional Keywords: guanosine endonuclease, p-granule, dimer, hydrolase
• Biological source: Caenorhabditis remanei
• Total number of polymer chains: 1
• Total formula weight: 28829.00

Authors

Aoki, S.T.,Bingman, C.A.,Wickens, M.,Kimble, J.E. (deposition date: 2015-07-25, release date: 2016-02-03, Last modification date: 2024-03-06)

Primary citation

Aoki, S.T.,Kershner, A.M.,Bingman, C.A.,Wickens, M.,Kimble, J.
PGL germ granule assembly protein is a base-specific, single-stranded RNase.
Proc.Natl.Acad.Sci.USA, 113:1279-1284, 2016

PubMed Abstract: 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 α-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.

PubMed: 26787882
DOI: 10.1073/pnas.1524400113

Experimental method

X-RAY DIFFRACTION (3.17014754005 Å)