2OOE

Crystal structure of HAT domain of murine CstF-77

Summary for 2OOE

• Entry DOI: 10.2210/pdb2ooe/pdb
• Related: 2OND
• Descriptor: Cleavage stimulation factor 77 kDa subunit (2 entities in total)
• Functional Keywords: hat domain, structural protein
• Biological source: Mus musculus (house mouse)
• Cellular location: Nucleus : Q99LI7
• Total number of polymer chains: 1
• Total formula weight: 62635.91

Authors

Bai, Y.,Auperin, T.C.,Chou, C.-Y.,Chang, G.-G.,Manley, J.L.,Tong, L. (deposition date: 2007-01-25, release date: 2007-04-10, Last modification date: 2023-12-27)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (3 Å)