5CV3

C. remanei PGL-1 Dimerization Domain - Hg

5CV3 の概要

• エントリーDOI: 10.2210/pdb5cv3/pdb
• 関連するPDBエントリー: 5COW
• 分子名称: Putative uncharacterized protein, ETHYL MERCURY ION (2 entities in total)
• 機能のキーワード: guanosine endonuclease, p-granule, dimer, hydrolase
• 由来する生物種: Caenorhabditis remanei
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 28829.00

構造登録者

Aoki, S.T.,Bingman, C.A.,Wickens, M.,Kimble, J.E. (登録日: 2015-07-25, 公開日: 2016-02-03, 最終更新日: 2024-03-06)

主引用文献

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

実験手法

X-RAY DIFFRACTION (3.17014754005 Å)