1HOW
THE X-RAY CRYSTAL STRUCTURE OF SKY1P, AN SR PROTEIN KINASE IN YEAST
Summary for 1HOW
| Entry DOI | 10.2210/pdb1how/pdb |
| Descriptor | SERINE/THREONINE-PROTEIN KINASE YMR216C, SULFATE ION, 1,2-ETHANEDIOL, ... (4 entities in total) |
| Functional Keywords | kinase, transferase |
| Biological source | Saccharomyces cerevisiae (baker's yeast) |
| Total number of polymer chains | 1 |
| Total formula weight | 43709.58 |
| Authors | Nolen, B.J.,Yun, C.Y.,Wong, C.F.,McCammon, J.A.,Fu, X.-D.,Ghosh, G. (deposition date: 2000-12-11, release date: 2001-02-28, Last modification date: 2024-02-07) |
| Primary citation | 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 Cited by 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: 11175909DOI: 10.1038/84178 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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