2OND

Crystal Structure of the HAT-C domain of murine CstF-77

2OND の概要

• エントリーDOI: 10.2210/pdb2ond/pdb
• 分子名称: Cleavage stimulation factor 77 kDa subunit (1 entity in total)
• 機能のキーワード: hat domain, structural protein
• 由来する生物種: Mus musculus (house mouse)
• 細胞内の位置: Nucleus : Q99LI7
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 73265.06

構造登録者

Bai, Y.,Auperin, T.C.,Chou, C.-Y.,Chang, G.-G.,Manley, J.L.,Tong, L. (登録日: 2007-01-23, 公開日: 2007-04-10, 最終更新日: 2024-10-30)

主引用文献

Bai, Y.,Auperin, T.C.,Chou, C.Y.,Chang, G.G.,Manley, J.L.,Tong, L.
Crystal Structure of Murine CstF-77: Dimeric Association and Implications for Polyadenylation of mRNA Precursors.
Mol.Cell, 25:863-875, 2007

PubMed Abstract: Cleavage stimulation factor (CstF) is a heterotrimeric protein complex essential for polyadenylation of mRNA precursors. The 77 kDa subunit, CstF-77, is known to mediate interactions with the other two subunits of CstF as well as with other components of the polyadenylation machinery. We report here the crystal structure of the HAT (half a TPR) domain of murine CstF-77, as well as its C-terminal subdomain. Structural and biochemical studies show that the HAT domain consists of two subdomains, HAT-N and HAT-C domains, with drastically different orientations of their helical motifs. The structures reveal a highly elongated dimer, spanning 165 A, with the dimerization mediated by the HAT-C domain. Light-scattering studies, yeast two-hybrid assays, and analytical ultracentrifugation measurements confirm this self-association. The mode of dimerization and the relative arrangement of the HAT-N and HAT-C domains are unique to CstF-77. Our data support a role for CstF dimerization in pre-mRNA 3' end processing.

PubMed: 17386263
DOI: 10.1016/j.molcel.2007.01.034

実験手法

X-RAY DIFFRACTION (2.8 Å)