| Literature DB >> 14656441 |
Qingping Xu1, Stace W Porter, Ann H West.
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.Entities:
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Year: 2003 PMID： 14656441 DOI： 10.1016/j.str.2003.10.016
Source DB: PubMed Journal: Structure ISSN： 0969-2126 Impact factor: 5.006