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1OXK

Complex between YPD1 and SLN1 response regulator domain in space group P3(2)

Summary for 1OXK
Entry DOI10.2210/pdb1oxk/pdb
Related1OXB 1QSP
DescriptorYpd1p, SLN1, SULFATE ION, ... (4 entities in total)
Functional Keywordsphosphorelay protein, two-component signaling protein, response regulator, hpt domain, histidine-containing phosphotransfer protein, ypd1p, sln1p, signaling protein
Biological sourceSaccharomyces cerevisiae (baker's yeast)
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Cellular locationCytoplasm: Q07688
Cell membrane; Multi-pass membrane protein (Potential): P39928
Total number of polymer chains12
Total formula weight206622.97
Authors
Xu, Q.,Porter, S.W.,West, A.H. (deposition date: 2003-04-02, release date: 2003-12-16, Last modification date: 2023-08-16)
Primary citationXu, Q.,Porter, S.W.,West, A.H.
The Yeast YPD1/SLN1 Complex. Insights into Molecular Recognition in Two-Component Signaling Systems.
Structure, 11:1569-1581, 2003
Cited by
PubMed Abstract: 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.
PubMed: 14656441
DOI: 10.1016/j.str.2003.10.016
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.1 Å)
Structure validation

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