The yeast YPD1/SLN1 complex: insights into molecular recognition in two-component signaling systems

Structure. 2003 Dec;11(12):1569-81. doi: 10.1016/j.str.2003.10.016.

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Binding Sites
  • Crystallography, X-Ray
  • DNA-Binding Proteins / chemistry*
  • Escherichia coli / metabolism
  • Intracellular Signaling Peptides and Proteins
  • Models, Molecular
  • Protein Binding
  • Protein Conformation
  • Protein Kinases / chemistry*
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Saccharomyces cerevisiae / enzymology*
  • Saccharomyces cerevisiae Proteins / chemistry*
  • Signal Transduction*

Substances

  • DNA-Binding Proteins
  • Intracellular Signaling Peptides and Proteins
  • Saccharomyces cerevisiae Proteins
  • Protein Kinases
  • YPD1 protein, S cerevisiae
  • SLN1 protein, S cerevisiae

Associated data

  • PDB/1OXB
  • PDB/1OXK