1bxm
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(New page: 200px<br /><applet load="1bxm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bxm, resolution 2.15Å" /> '''ENGINEERED BETA-CRYP...)
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Revision as of 09:52, 20 November 2007
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ENGINEERED BETA-CRYPTOGEIN COMPLEXED WITH ERGOSTEROL
Overview
Elicitins, produced by most of the phytopathogenic fungi of the genus, Phytophthora, provoke in tobacco both remote leaf necrosis and the, induction of a resistance against subsequent attack by various, microorganisms. Despite the recent description of the three-dimensional, crystal structure of cryptogein (CRY), the molecular basis of the, interactions between Phytophthora and plants largely remains unknown. The, X-ray crystal structure, refined at 2.1 A, of a ligand complexed, mutated, CRY, K13H, is reported. Analysis of this structure reveals that CRY is, able to encapsulate a ligand that induces only a minor conformational, change in the protein structure. The ligand has been identified as an, ergosterol by gas chromatographic analysis coupled with mass spectrometry, analysis. This result is consistent with biochemical data that have shown, that elicitins are a distinct class of Sterol Carrier Proteins (SCP). Data, presented here provide the first structural description of the pertinent, features of the elicitin sterol interaction and permit a reassessment of, the importance of both the key residue 13 and the mobility of the omega, loop for the accessibility of the sterol to the cavity. The biological, implications thereof are discussed. This paper reports the first structure, of a SCP/sterol complex.
About this Structure
1BXM is a Single protein structure of sequence from Phytophthora cryptogea with ERG as ligand. Full crystallographic information is available from OCA.
Reference
The 2.1 A structure of an elicitin-ergosterol complex: a recent addition to the Sterol Carrier Protein family., Boissy G, O'Donohue M, Gaudemer O, Perez V, Pernollet JC, Brunie S, Protein Sci. 1999 Jun;8(6):1191-9. PMID:10386869
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