Abstract
'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 Ypd1y, a key intermediate in the osmosensing multistep phosphorelay signal transduction, catalyzes the phosphoryl group transfer between response regulators. Its 1.8 Å 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.
| Original language | English |
|---|---|
| Pages (from-to) | 753-761 |
| Number of pages | 9 |
| Journal | Journal of Molecular Biology |
| Volume | 293 |
| Issue number | 4 |
| DOIs | |
| Publication status | Published - 1999 Nov 5 |
| Externally published | Yes |
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Keywords
- Crystal structure
- Phosphorelay phosphotransferase
- Saccharomyces cerevisiae
- Signal transduction
- Ypd1p
ASJC Scopus subject areas
- Virology
Cite this
Insights into eukaryotic multistep phosphorelay signal transduction revealed by the crystal structure of Ypd1p from Saccharomyces cerevisiae. / Song, Hyun Kyu; Lee, Jae Young; Lee, Myong Gyong; Moon, Jinho; Min, Kyeongsik; Yang, Jin Kuk; Suh, Se Won.
In: Journal of Molecular Biology, Vol. 293, No. 4, 05.11.1999, p. 753-761.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Insights into eukaryotic multistep phosphorelay signal transduction revealed by the crystal structure of Ypd1p from Saccharomyces cerevisiae
AU - Song, Hyun Kyu
AU - Lee, Jae Young
AU - Lee, Myong Gyong
AU - Moon, Jinho
AU - Min, Kyeongsik
AU - Yang, Jin Kuk
AU - Suh, Se Won
PY - 1999/11/5
Y1 - 1999/11/5
N2 - '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 Ypd1y, a key intermediate in the osmosensing multistep phosphorelay signal transduction, catalyzes the phosphoryl group transfer between response regulators. Its 1.8 Å 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.
AB - '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 Ypd1y, a key intermediate in the osmosensing multistep phosphorelay signal transduction, catalyzes the phosphoryl group transfer between response regulators. Its 1.8 Å 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.
KW - Crystal structure
KW - Phosphorelay phosphotransferase
KW - Saccharomyces cerevisiae
KW - Signal transduction
KW - Ypd1p
UR - http://www.scopus.com/inward/record.url?scp=0033527581&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0033527581&partnerID=8YFLogxK
U2 - 10.1006/jmbi.1999.3215
DO - 10.1006/jmbi.1999.3215
M3 - Article
C2 - 10543964
AN - SCOPUS:0033527581
VL - 293
SP - 753
EP - 761
JO - Journal of Molecular Biology
JF - Journal of Molecular Biology
SN - 0022-2836
IS - 4
ER -