3BAP

Crystal Structure of the 25 kDa Subunit of Human Cleavage Factor Im

Summary for 3BAP

• Entry DOI: 10.2210/pdb3bap/pdb
• Related: 2Cl3 2j8q
• Descriptor: Cleavage and polyadenylation specificity factor subunit 5, GLYCEROL (3 entities in total)
• Functional Keywords: cpsf5, rna processing, cleavage factor, mrna processing, nucleus, phosphoprotein, rna-binding, rna binding protein
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus : O43809
• Total number of polymer chains: 1
• Total formula weight: 26538.92

Authors

Coseno, M.,Doublie, S. (deposition date: 2007-11-08, release date: 2008-02-19, Last modification date: 2024-10-30)

Primary citation

Coseno, M.,Martin, G.,Berger, C.,Gilmartin, G.,Keller, W.,Doublie, S.
Crystal structure of the 25 kDa subunit of human cleavage factor Im.
Nucleic Acids Res., 36:3474-3483, 2008

PubMed Abstract: Cleavage factor I(m) is an essential component of the pre-messenger RNA 3'-end processing machinery in higher eukaryotes, participating in both the polyadenylation and cleavage steps. Cleavage factor I(m) is an oligomer composed of a small 25 kDa subunit (CF I(m)25) and a variable larger subunit of either 59, 68 or 72 kDa. The small subunit also interacts with RNA, poly(A) polymerase, and the nuclear poly(A)-binding protein. These protein-protein interactions are thought to be facilitated by the Nudix domain of CF I(m)25, a hydrolase motif with a characteristic alpha/beta/alpha fold and a conserved catalytic sequence or Nudix box. We present here the crystal structures of human CF I(m)25 in its free and diadenosine tetraphosphate (Ap(4)A) bound forms at 1.85 and 1.80 A, respectively. CF I(m)25 crystallizes as a dimer and presents the classical Nudix fold. Results from crystallographic and biochemical experiments suggest that CF I(m)25 makes use of its Nudix fold to bind but not hydrolyze ATP and Ap(4)A. The complex and apo protein structures provide insight into the active oligomeric state of CF I(m) and suggest a possible role of nucleotide binding in either the polyadenylation and/or cleavage steps of pre-messenger RNA 3'-end processing.

PubMed: 18445629
DOI: 10.1093/nar/gkn079

Experimental method

X-RAY DIFFRACTION (1.85 Å)