1how: Difference between revisions

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[[Image:1how.gif|left|200px]]<br /><applet load="1how" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1how.gif|left|200px]]<br /><applet load="1how" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1how, resolution 2.1Å" />

'''THE X-RAY CRYSTAL STRUCTURE OF SKY1P, AN SR PROTEIN KINASE IN YEAST'''<br />

==Overview==

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.

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 Structure==

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 SO4 and EDO as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1HOW OCA].

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].

==Reference==

Line 13:

[[Category: Saccharomyces cerevisiae]]

[[Category: Single protein]]

[[Category: Fu, X.D.]]

[[Category: Fu, X D.]]

[[Category: Ghosh, G.]]

[[Category: McCammon, J.A.]]

[[Category: McCammon, J A.]]

[[Category: Nolen, B.J.]]

[[Category: Nolen, B J.]]

[[Category: Wong, C.F.]]

[[Category: Wong, C F.]]

[[Category: Yun, C.Y.]]

[[Category: Yun, C Y.]]

[[Category: EDO]]

[[Category: SO4]]

[[Category: kinase]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov 20 16~~:43:~~01 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:03:21 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1how.gif|left|200px]]<br /><applet load="1how" size="450" color="white" frame="true" align="right" spinBox="true"
+[[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==
-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.
+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 Structure==
-HOW 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 SO4 and EDO as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HOW OCA].
+HOW 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].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Saccharomyces cerevisiae]]
 [[Category: Single protein]]
-[[Category: Fu, X.D.]]
+[[Category: Fu, X D.]]
 [[Category: Ghosh, G.]]
-[[Category: McCammon, J.A.]]
+[[Category: McCammon, J A.]]
-[[Category: Nolen, B.J.]]
+[[Category: Nolen, B J.]]
-[[Category: Wong, C.F.]]
+[[Category: Wong, C F.]]
-[[Category: Yun, C.Y.]]
+[[Category: Yun, C Y.]]
 [[Category: EDO]]
 [[Category: SO4]]
 [[Category: kinase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:43:01 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:03:21 2008''