1how: Difference between revisions
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|PDB= 1how |SIZE=350|CAPTION= <scene name='initialview01'>1how</scene>, resolution 2.1Å | |PDB= 1how |SIZE=350|CAPTION= <scene name='initialview01'>1how</scene>, resolution 2.1Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand= | |LIGAND= <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= YMR216C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]) | |GENE= YMR216C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]) | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1how FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1how OCA], [http://www.ebi.ac.uk/pdbsum/1how PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1how RCSB]</span> | |||
}} | }} | ||
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[[Category: Wong, C F.]] | [[Category: Wong, C F.]] | ||
[[Category: Yun, C Y.]] | [[Category: Yun, C Y.]] | ||
[[Category: kinase]] | [[Category: kinase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:08:27 2008'' | ||
Revision as of 21:08, 30 March 2008
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| , resolution 2.1Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | YMR216C (Saccharomyces cerevisiae) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THE X-RAY CRYSTAL STRUCTURE OF SKY1P, AN SR PROTEIN KINASE IN YEAST
OverviewOverview
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 StructureAbout this Structure
1HOW is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
ReferenceReference
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
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