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1how

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Revision as of 07:26, 7 April 2021

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

Structural highlights

1how is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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.

Publication Abstract from PubMed

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.

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^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ 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
↑ 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

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1how"

@@ Line 3: / Line 3: @@
 <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. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HOW FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1how]] is a 1 chain structure. 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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+</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'>[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://pdbe.org/1how PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1how RCSB], [http://www.ebi.ac.uk/pdbsum/1how PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1how ProSAT]</span></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 ==
-[[http://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>
+[[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]]
@@ Line 30: / Line 30: @@
 ==See Also==
-*[[Serine/threonine protein kinase|Serine/threonine protein kinase]]
+*[[Serine/threonine protein kinase 3D structures|Serine/threonine protein kinase 3D structures]]
 == References ==
 <references/>

1how

From Proteopedia

Revision as of 07:26, 7 April 2021

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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