1oxb
From Proteopedia
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Complex between YPD1 and SLN1 response regulator domain in space group P2(1)2(1)2(1)
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
1OXB is a Protein complex structure of sequences from Saccharomyces cerevisiae with SO4 as ligand. 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
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