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1oxb

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(New page: 200px<br /><applet load="1oxb" size="450" color="white" frame="true" align="right" spinBox="true" caption="1oxb, resolution 2.30&Aring;" /> '''Complex between YPD1...)
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[[Image:1oxb.jpg|left|200px]]<br /><applet load="1oxb" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1oxb.jpg|left|200px]]<br /><applet load="1oxb" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1oxb, resolution 2.30&Aring;" />
caption="1oxb, resolution 2.30&Aring;" />
'''Complex between YPD1 and SLN1 response regulator domain in space group P2(1)2(1)2(1)'''<br />
'''Complex between YPD1 and SLN1 response regulator domain in space group P2(1)2(1)2(1)'''<br />
==Overview==
==Overview==
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In Saccharomyces cerevisiae, a branched multistep phosphorelay signaling, pathway regulates cellular adaptation to hyperosmotic stress. YPD1, functions as a histidine-phosphorylated protein intermediate required for, phosphoryl group transfer from a membrane-bound sensor histidine kinase, (SLN1) to two distinct response regulator proteins (SSK1 and SKN7). These, four proteins are evolutionarily related to the well-characterized, "two-component" regulatory proteins from bacteria. Although structural, information is available for many two-component signaling proteins, there, are very few examples of complexes between interacting phosphorelay, partners. Here we report the first crystal structure of a prototypical, monomeric histidine-containing phosphotransfer (HPt) protein YPD1 in, complex with its upstream phosphodonor, the response regulator domain, associated with SLN1.
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In Saccharomyces cerevisiae, a branched multistep phosphorelay signaling pathway regulates cellular adaptation to hyperosmotic stress. YPD1 functions as a histidine-phosphorylated protein intermediate required for phosphoryl group transfer from a membrane-bound sensor histidine kinase (SLN1) to two distinct response regulator proteins (SSK1 and SKN7). These four proteins are evolutionarily related to the well-characterized "two-component" regulatory proteins from bacteria. Although structural information is available for many two-component signaling proteins, there are very few examples of complexes between interacting phosphorelay partners. Here we report the first crystal structure of a prototypical monomeric histidine-containing phosphotransfer (HPt) protein YPD1 in complex with its upstream phosphodonor, the response regulator domain associated with SLN1.
==About this Structure==
==About this Structure==
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1OXB is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OXB OCA].
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1OXB is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OXB OCA].
==Reference==
==Reference==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Porter, S.W.]]
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[[Category: Porter, S W.]]
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[[Category: West, A.H.]]
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[[Category: West, A H.]]
[[Category: Xu, Q.]]
[[Category: Xu, Q.]]
[[Category: SO4]]
[[Category: SO4]]
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[[Category: ypd1p]]
[[Category: ypd1p]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:16:28 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:22:47 2008''

Revision as of 12:22, 21 February 2008


1oxb, resolution 2.30Å

Drag the structure with the mouse to rotate

Complex between YPD1 and SLN1 response regulator domain in space group P2(1)2(1)2(1)

Overview

In Saccharomyces cerevisiae, a branched multistep phosphorelay signaling pathway regulates cellular adaptation to hyperosmotic stress. YPD1 functions as a histidine-phosphorylated protein intermediate required for phosphoryl group transfer from a membrane-bound sensor histidine kinase (SLN1) to two distinct response regulator proteins (SSK1 and SKN7). These four proteins are evolutionarily related to the well-characterized "two-component" regulatory proteins from bacteria. Although structural information is available for many two-component signaling proteins, there are very few examples of complexes between interacting phosphorelay partners. Here we report the first crystal structure of a prototypical monomeric histidine-containing phosphotransfer (HPt) protein YPD1 in complex with its upstream phosphodonor, the response regulator domain associated with SLN1.

About this Structure

1OXB is a Protein complex structure of sequences from Saccharomyces cerevisiae with as ligand. Full crystallographic information is available from OCA.

Reference

The yeast YPD1/SLN1 complex: insights into molecular recognition in two-component signaling systems., Xu Q, Porter SW, West AH, Structure. 2003 Dec;11(12):1569-81. PMID:14656441

Page seeded by OCA on Thu Feb 21 14:22:47 2008

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