3BEG

Crystal structure of SR protein kinase 1 complexed to its substrate ASF/SF2

Summary for 3BEG

• Entry DOI: 10.2210/pdb3beg/pdb
• Descriptor: Serine/threonine-protein kinase SRPK1, Splicing factor, arginine/serine-rich 1, PHOSPHOSERINE, ... (5 entities in total)
• Functional Keywords: kinase, sr protein kinase, sr protein, pre-mrna splicing, atp-binding, chromosome partition, differentiation, mrna processing, nucleotide-binding, nucleus, phosphoprotein, serine/threonine-protein kinase, transferase, methylation, rna-binding, spliceosome, transferase-splicing complex, transferase/splicing
• Biological source: Homo sapiens (human); More
• Cellular location: Isoform 2: Cytoplasm. Isoform 1: Cytoplasm: Q96SB4; Cytoplasm : Q07955
• Total number of polymer chains: 2
• Total formula weight: 57183.68

Authors

Ngo, J.C.,Giang, K.,Chakrabarti, S.,Ma, C.-T.,Huynh, N.,Hagopian, J.,Dorrestein, P.C.,Fu, X.-D.,Adams, J.A.,Ghosh, G. (deposition date: 2007-11-18, release date: 2008-04-01, Last modification date: 2024-02-21)

Primary citation

Ngo, J.C.,Giang, K.,Chakrabarti, S.,Ma, C.-T.,Huynh, N.,Hagopian, J.,Dorrestein, P.C.,Fu, X.-D.,Adams, J.A.,Ghosh, G.
A sliding docking interaction is essential for sequential and processive phosphorylation of an SR protein by SRPK1
Mol.Cell, 29:563-576, 2008

PubMed Abstract: The 2.9 A crystal structure of the core SRPK1:ASF/SF2 complex reveals that the N-terminal half of the basic RS domain of ASF/SF2, which is destined to be phosphorylated, is bound to an acidic docking groove of SRPK1 distal to the active site. Phosphorylation of ASF/SF2 at a single site in the C-terminal end of the RS domain generates a primed phosphoserine that binds to a basic site in the kinase. Biochemical experiments support a directional sliding of the RS peptide through the docking groove to the active site during phosphorylation, which ends with the unfolding of a beta strand of the RRM domain and binding of the unfolded region to the docking groove. We further suggest that the priming of the first serine facilitates directional substrate translocation and efficient phosphorylation.

PubMed: 18342604
DOI: 10.1016/j.molcel.2007.12.017

Experimental method

X-RAY DIFFRACTION (2.9 Å)