1oxk
From Proteopedia
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| - | [[Image:1oxk.gif|left|200px]] | + | [[Image:1oxk.gif|left|200px]] |
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| - | '''Complex between YPD1 and SLN1 response regulator domain in space group P3(2)''' | + | {{Structure |
| + | |PDB= 1oxk |SIZE=350|CAPTION= <scene name='initialview01'>1oxk</scene>, resolution 2.10Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= YPD1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]), SLN1 OR YPD2 OR YIL147C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]) | ||
| + | }} | ||
| + | |||
| + | '''Complex between YPD1 and SLN1 response regulator domain in space group P3(2)''' | ||
| + | |||
| + | |||
| + | ==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== | ==About this Structure== | ||
| - | 1OXK is a [ | + | 1OXK is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OXK OCA]. |
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| + | ==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:[http://www.ncbi.nlm.nih.gov/pubmed/14656441 14656441] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
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[[Category: ypd1p]] | [[Category: ypd1p]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:16:59 2008'' |
Revision as of 11:17, 20 March 2008
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| , resolution 2.10Å | |||||||
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| Ligands: | |||||||
| Gene: | YPD1 (Saccharomyces cerevisiae), SLN1 OR YPD2 OR YIL147C (Saccharomyces cerevisiae) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Complex between YPD1 and SLN1 response regulator domain in space group P3(2)
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
1OXK is a Protein complex structure of sequences from Saccharomyces cerevisiae. 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 Mar 20 13:16:59 2008
