1oxb
Complex between YPD1 and SLN1 response regulator domain in space group P2(1)2(1)2(1)
OverviewOverview
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 StructureAbout this Structure
1OXB is a Protein complex structure of sequences from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
ReferenceReference
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 Sat May 3 04:23:32 2008