1c02

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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1c02 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c02 OCA], [http://www.ebi.ac.uk/pdbsum/1c02 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1c02 RCSB]</span>
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Revision as of 16:11, 30 March 2008


PDB ID 1c02

Drag the structure with the mouse to rotate
, resolution 1.8Å
Related: 2A0B


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF YEAST YPD1P


Overview

"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 Structure

1C02 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

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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