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| | <StructureSection load='1oxb' size='340' side='right'caption='[[1oxb]], [[Resolution|resolution]] 2.30Å' scene=''> | | <StructureSection load='1oxb' size='340' side='right'caption='[[1oxb]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1oxb]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OXB OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1OXB FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1oxb]] is a 2 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=1OXB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OXB FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1qsp|1qsp]], [[1oxk|1oxk]]</div></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">YPD1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824]), SLN1 OR YPD2 OR YIL147C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</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=1oxb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oxb OCA], [https://pdbe.org/1oxb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1oxb RCSB], [https://www.ebi.ac.uk/pdbsum/1oxb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1oxb ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1oxb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oxb OCA], [http://pdbe.org/1oxb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1oxb RCSB], [http://www.ebi.ac.uk/pdbsum/1oxb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1oxb ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/YPD1_YEAST YPD1_YEAST]] Phosphorelay intermediate protein that is part of the branched SLN1-YPD1-SKN7/SSK1 two-component regulatory system, which controls activity of the HOG1 pathway and gene expression in response to changes in the osmolarity of the extracellular environment. Catalyzes the phosphoryl group transfer from the membrane-bound osmosensing histidine kinase SLN1 to two distinct response regulator proteins, SSK1 in the cytoplasm, and transcription factor SKN7 in the nucleus.<ref>PMID:11073911</ref> <ref>PMID:9843501</ref> [[http://www.uniprot.org/uniprot/SLN1_YEAST SLN1_YEAST]] Histidine kinase that acts as a osmosensor at the plasma membrane. Part of the bifurcated SLN1-YPD1-SKN7/SSK1 two-component regulatory system, which controls activity of the HOG1 pathway and gene expression in response to changes in the osmolarity of the extracellular environment. Under normal osmotic conditions, the histidine kinase autophosphorylates His-576. This phosphate is subsequently transferred to Asp-1144, from where it is relayed to 'His-64' of the phosphorelay intermediate protein YPD1. Under high osmolarity conditions, the histidine kinase is no longer active.<ref>PMID:8808622</ref> <ref>PMID:9843501</ref> | + | [https://www.uniprot.org/uniprot/YPD1_YEAST YPD1_YEAST] Phosphorelay intermediate protein that is part of the branched SLN1-YPD1-SKN7/SSK1 two-component regulatory system, which controls activity of the HOG1 pathway and gene expression in response to changes in the osmolarity of the extracellular environment. Catalyzes the phosphoryl group transfer from the membrane-bound osmosensing histidine kinase SLN1 to two distinct response regulator proteins, SSK1 in the cytoplasm, and transcription factor SKN7 in the nucleus.<ref>PMID:11073911</ref> <ref>PMID:9843501</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 18824]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Porter, S W]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: West, A H]] | + | [[Category: Porter SW]] |
| - | [[Category: Xu, Q]] | + | [[Category: West AH]] |
| - | [[Category: Histidine-containing phosphotransfer protein]] | + | [[Category: Xu Q]] |
| - | [[Category: Hpt domain]]
| + | |
| - | [[Category: Phosphorelay protein]]
| + | |
| - | [[Category: Response regulator]]
| + | |
| - | [[Category: Signaling protein]]
| + | |
| - | [[Category: Sln1p]]
| + | |
| - | [[Category: Two-component signaling protein]]
| + | |
| - | [[Category: Ypd1p]]
| + | |
| Structural highlights
Function
YPD1_YEAST Phosphorelay intermediate protein that is part of the branched SLN1-YPD1-SKN7/SSK1 two-component regulatory system, which controls activity of the HOG1 pathway and gene expression in response to changes in the osmolarity of the extracellular environment. Catalyzes the phosphoryl group transfer from the membrane-bound osmosensing histidine kinase SLN1 to two distinct response regulator proteins, SSK1 in the cytoplasm, and transcription factor SKN7 in the nucleus.[1] [2]
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
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.
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[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Janiak-Spens F, Sparling DP, West AH. Novel role for an HPt domain in stabilizing the phosphorylated state of a response regulator domain. J Bacteriol. 2000 Dec;182(23):6673-8. PMID:11073911
- ↑ Li S, Ault A, Malone CL, Raitt D, Dean S, Johnston LH, Deschenes RJ, Fassler JS. The yeast histidine protein kinase, Sln1p, mediates phosphotransfer to two response regulators, Ssk1p and Skn7p. EMBO J. 1998 Dec 1;17(23):6952-62. PMID:9843501 doi:http://dx.doi.org/10.1093/emboj/17.23.6952
- ↑ Xu Q, Porter SW, West AH. The yeast YPD1/SLN1 complex: insights into molecular recognition in two-component signaling systems. Structure. 2003 Dec;11(12):1569-81. PMID:14656441
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