1HOW

THE X-RAY CRYSTAL STRUCTURE OF SKY1P, AN SR PROTEIN KINASE IN YEAST

1HOW の概要

• エントリーDOI: 10.2210/pdb1how/pdb
• 分子名称: SERINE/THREONINE-PROTEIN KINASE YMR216C, SULFATE ION, 1,2-ETHANEDIOL, ... (4 entities in total)
• 機能のキーワード: kinase, transferase
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 43709.58

構造登録者

Nolen, B.J.,Yun, C.Y.,Wong, C.F.,McCammon, J.A.,Fu, X.-D.,Ghosh, G. (登録日: 2000-12-11, 公開日: 2001-02-28, 最終更新日: 2024-02-07)

主引用文献

Nolen, B.,Yun, C.Y.,Wong, C.F.,McCammon, J.A.,Fu, X.D.,Ghosh, G.
The structure of Sky1p reveals a novel mechanism for constitutive activity.
Nat.Struct.Biol., 8:176-183, 2001

PubMed Abstract: 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.

PubMed: 11175909
DOI: 10.1038/84178

実験手法

X-RAY DIFFRACTION (2.1 Å)