1oxb | pdb_00001oxb
Complex between YPD1 and SLN1 response regulator domain in space group P2(1)2(1)2(1)
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] [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 Under high osmolarity conditions, the histidine kinase is no longer active.[3] [4] Evolutionary Conservation Check, as determined by ConSurfDB.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 PubMedIn 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[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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