1c03
CRYSTAL STRUCTURE OF YPD1P (TRICLINIC FORM)
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OverviewOverview
"Two-component" phosphorelay signal transduction systems constitute a, potential target for antibacterial and antifungal agents, since they are, found exclusively in prokaryotes and lower eukaryotes (yeast, fungi, slime, mold, and plants) but not in mammalian organisms. Saccharomyces cerevisiae, Ypd1p, a key intermediate in the osmosensing multistep phosphorelay signal, transduction, catalyzes the phosphoryl group transfer between response, regulators. Its 1.8 A structure, representing the first example of a, eukaryotic phosphorelay protein, contains a four-helix bundle as in the, HPt domain of Escherichia coli ArcB sensor kinase. However, Ypd1p has a, 44-residue insertion between the last two helices of the helix bundle. The, side-chain of His64, the site of phosphorylation, protrudes into the, solvent. The structural resemblance between Ypd1p and ArcB HPt domain, suggests that both prokaryotes and lower eukaryotes utilize the same basic, protein fold for phosphorelay signal transduction. This study sheds light, on the best characterized eukaryotic phosphorelay system.
About this StructureAbout this Structure
1C03 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
ReferenceReference
Insights into eukaryotic multistep phosphorelay signal transduction revealed by the crystal structure of Ypd1p from Saccharomyces cerevisiae., Song HK, Lee JY, Lee MG, Moon J, Min K, Yang JK, Suh SW, J Mol Biol. 1999 Nov 5;293(4):753-61. PMID:10543964
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