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[[Image:1how.gif|left|200px]]<br /><applet load="1how" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1how, resolution 2.1&Aring;" />
'''THE X-RAY CRYSTAL STRUCTURE OF SKY1P, AN SR PROTEIN KINASE IN YEAST'''<br />


==Overview==
==THE X-RAY CRYSTAL STRUCTURE OF SKY1P, AN SR PROTEIN KINASE IN YEAST==
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.
<StructureSection load='1how' size='340' side='right'caption='[[1how]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1how]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HOW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HOW FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1how FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1how OCA], [https://pdbe.org/1how PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1how RCSB], [https://www.ebi.ac.uk/pdbsum/1how PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1how ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SKY1_YEAST SKY1_YEAST] Constitutively active kinase, specifically and sequentially phosphorylates serine/arginine (SR)-type shuttling mRNA binding proteins in their RS dipeptide repeats.<ref>PMID:11175909</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ho/1how_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1how ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1HOW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=EDO:'>EDO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HOW OCA].
*[[Serine/threonine protein kinase 3D structures|Serine/threonine protein kinase 3D structures]]
 
== References ==
==Reference==
<references/>
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11175909 11175909]
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Fu X-D]]
[[Category: Fu, X D.]]
[[Category: Ghosh G]]
[[Category: Ghosh, G.]]
[[Category: McCammon JA]]
[[Category: McCammon, J A.]]
[[Category: Nolen BJ]]
[[Category: Nolen, B J.]]
[[Category: Wong CF]]
[[Category: Wong, C F.]]
[[Category: Yun CY]]
[[Category: Yun, C Y.]]
[[Category: EDO]]
[[Category: SO4]]
[[Category: kinase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:03:21 2008''

Latest revision as of 10:29, 7 February 2024

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

Structural highlights

1how is a 1 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.1Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SKY1_YEAST Constitutively active kinase, specifically and sequentially phosphorylates serine/arginine (SR)-type shuttling mRNA binding proteins in their RS dipeptide repeats.[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Nolen B, Yun CY, Wong CF, McCammon JA, Fu XD, Ghosh G. The structure of Sky1p reveals a novel mechanism for constitutive activity. Nat Struct Biol. 2001 Feb;8(2):176-83. PMID:11175909 doi:10.1038/84178

1how, resolution 2.10Å

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