2a8f

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(New page: 200px<br /><applet load="2a8f" size="450" color="white" frame="true" align="right" spinBox="true" caption="2a8f, resolution 1.35&Aring;" /> '''beta-cinnamomin afte...)
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[[Image:2a8f.gif|left|200px]]<br /><applet load="2a8f" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2a8f, resolution 1.35&Aring;" />
caption="2a8f, resolution 1.35&Aring;" />
'''beta-cinnamomin after sterol removal'''<br />
'''beta-cinnamomin after sterol removal'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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2A8F is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Phytophthora_cinnamomi Phytophthora cinnamomi]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2A8F OCA].
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2A8F is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Phytophthora_cinnamomi Phytophthora cinnamomi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A8F OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Archer, M.]]
[[Category: Archer, M.]]
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[[Category: Baptista, R.P.]]
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[[Category: Baptista, R P.]]
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[[Category: Carrondo, M.A.]]
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[[Category: Carrondo, M A.]]
[[Category: Cravador, A.]]
[[Category: Cravador, A.]]
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[[Category: Enguita, F.J.]]
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[[Category: Enguita, F J.]]
[[Category: Martel, P.]]
[[Category: Martel, P.]]
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[[Category: Melo, E.P.]]
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[[Category: Melo, E P.]]
[[Category: Miranda, S.]]
[[Category: Miranda, S.]]
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[[Category: Rodrigues, M.L.]]
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[[Category: Rodrigues, M L.]]
[[Category: Sousa, N.]]
[[Category: Sousa, N.]]
[[Category: Thomaz, M.]]
[[Category: Thomaz, M.]]
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[[Category: sterol carrier protein]]
[[Category: sterol carrier protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 07:59:10 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:24:39 2008''

Revision as of 14:24, 21 February 2008


2a8f, resolution 1.35Å

Drag the structure with the mouse to rotate

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

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