1how
From Proteopedia
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THE X-RAY CRYSTAL STRUCTURE OF SKY1P, AN SR PROTEIN KINASE IN YEAST
Overview
Sky1p is the only member of the SR protein kinase (SRPK) family in, Saccharomyces cerevisiae. SRPKs are constitutively active kinases that, display remarkable substrate specificity and have been implicated in RNA, processing. Here we present the three-dimensional structure of a fully, active truncated Sky1p. Analysis of the structure and structure-based, functional studies reveal that the C-terminal tail, an unusual Glu residue, located in the P+1 loop, and a unique mechanism for the positioning of, helix alpha C act together to render Sky1p constitutively active. We have, modeled a substrate peptide bound to Sky1p. The modeled complex combined, with mutagenesis studies illustrate the molecular basis for substrate, recognition by this kinase and suggest a mechanism by which SRPKs catalyze, a sequential phosphorylation reaction of the consecutive RS dipeptide, repeats characteristic of mammalian SRPK substrates.
About this Structure
1HOW is a Single protein structure of sequence from Saccharomyces cerevisiae with SO4 and EDO as ligands. Full crystallographic information is available from OCA.
Reference
The structure of Sky1p reveals a novel mechanism for constitutive activity., Nolen B, Yun CY, Wong CF, McCammon JA, Fu XD, Ghosh G, Nat Struct Biol. 2001 Feb;8(2):176-83. PMID:11175909
Page seeded by OCA on Tue Nov 20 16:43:01 2007
Categories: Saccharomyces cerevisiae | Single protein | Fu, X.D. | Ghosh, G. | McCammon, J.A. | Nolen, B.J. | Wong, C.F. | Yun, C.Y. | EDO | SO4 | Kinase
