2a8f
From Proteopedia
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beta-cinnamomin after sterol removal
Overview
The crystal structure of the elicitin beta-cinnamomin (beta-CIN) was, determined in complex with ergosterol at 1.1 A resolution., beta-CIN/ergosterol complex crystallized in the monoclinic space group, P2(1), with unit cell parameters of a = 31.0, b = 62.8, c = 50.0 A and, beta = 93.4 degrees and two molecules in the asymmetric unit. Ligand, extraction with chloroform followed by crystallographic analysis yielded a, 1.35 A structure of beta-CIN (P4(3)2(1)2 space group) where the, characteristic elicitin fold was kept. After incubation with cholesterol, a new complex structure was obtained, showing that the protein retains, after the extraction procedure, its ability to complex sterols. The, necrotic effect of beta-CIN on tobacco was also shown to remain unchanged., Theoretical docking studies of the triterpene lupeol to beta-CIN provided, an explanation for the apparent inability of beta-CIN to bind this ligand, as observed experimentally.
About this Structure
2A8F is a Single protein structure of sequence from Phytophthora cinnamomi. Full crystallographic information is available from OCA.
Reference
Crystal structures of the free and sterol-bound forms of beta-cinnamomin., Rodrigues ML, Archer M, Martel P, Miranda S, Thomaz M, Enguita FJ, Baptista RP, Pinho e Melo E, Sousa N, Cravador A, Carrondo MA, Biochim Biophys Acta. 2006 Jan;1764(1):110-21. Epub 2005 Oct 6. PMID:16249127
Page seeded by OCA on Wed Nov 21 07:59:10 2007
