The 1.45 A resolution structure of the cryptogein-cholesterol complex: a close-up view of a sterol carrier protein (SCP) active site
| Autor: | Michel Ponchet, Marie Bernard Lascombe, Paul Venard, Thierry Prangé, Jean Pierre Blein, Marie Louise Milat |
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| Rok vydání: | 2002 |
| Předmět: |
Models
Molecular Stereochemistry Molecular Sequence Data Biology Fungal Proteins chemistry.chemical_compound Structural Biology Amino Acid Sequence Oomycete Binding Sites Molecular Structure Sequence Homology Amino Acid Cholesterol Phytophthora cryptogea Resolution (electron density) Algal Proteins Active site General Medicine biology.organism_classification Sterol Elicitor Sterols Sterol carrier protein Biochemistry chemistry biology.protein Carrier Proteins |
| Zdroj: | Acta crystallographica. Section D, Biological crystallography. 58(Pt 9) |
| ISSN: | 0907-4449 |
| Popis: | Cryptogein is a small 10 kDa elicitor produced by the phytoparasitic oomycete Phytophthora cryptogea. The protein also displays a sterol carrier activity. The native protein crystallizes in space group P4(1)22, with unit-cell parameters a = b = 46.51, c = 134.9 A (diffraction limit: 2.1 A). Its complex with cholesterol crystallizes in space group C222(1), with unit-cell parameters a = 30.96, b = 94.8, c = 65.3 A and a resolution enhanced to 1.45 A. The large inner non-specific hydrophobic cavity is able to accommodate a large variety of 3-beta-hydroxy sterols. Cryptogein probably acts as a sterol shuttle helping the pathogen to grow and complete its life cycle. |
| Databáze: | OpenAIRE |
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