1c02

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(New page: 200px<br /><applet load="1c02" size="450" color="white" frame="true" align="right" spinBox="true" caption="1c02, resolution 1.8&Aring;" /> '''CRYSTAL STRUCTURE OF ...)
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[[Image:1c02.gif|left|200px]]<br /><applet load="1c02" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1c02, resolution 1.8&Aring;" />
caption="1c02, resolution 1.8&Aring;" />
'''CRYSTAL STRUCTURE OF YEAST YPD1P'''<br />
'''CRYSTAL STRUCTURE OF YEAST YPD1P'''<br />
==Overview==
==Overview==
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"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.
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"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==
==About this Structure==
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1C02 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1C02 OCA].
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1C02 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C02 OCA].
==Reference==
==Reference==
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[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Lee, J.Y.]]
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[[Category: Lee, J Y.]]
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[[Category: Lee, M.G.]]
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[[Category: Lee, M G.]]
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[[Category: Song, H.K.]]
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[[Category: Song, H K.]]
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[[Category: Suh, S.W.]]
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[[Category: Suh, S W.]]
[[Category: helix-bundle]]
[[Category: helix-bundle]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:03:08 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:00:58 2008''

Revision as of 10:01, 21 February 2008


1c02, resolution 1.8Å

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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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