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| {{STRUCTURE_1c03| PDB=1c03 | SCENE= }} | | {{STRUCTURE_1c03| PDB=1c03 | SCENE= }} |
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| '''CRYSTAL STRUCTURE OF YPD1P (TRICLINIC FORM)'''
| | ===CRYSTAL STRUCTURE OF YPD1P (TRICLINIC FORM)=== |
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| ==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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_10543964}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 10543964 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_10543964}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Four helical bundle]] | | [[Category: Four helical bundle]] |
| [[Category: Signal transduction]] | | [[Category: Signal transduction]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:10:25 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 20:01:25 2008'' |
