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2aib
From Proteopedia
(New page: 200px<br /><applet load="2aib" size="450" color="white" frame="true" align="right" spinBox="true" caption="2aib, resolution 1.10Å" /> '''beta-cinnamomin in c...) |
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| - | [[Image:2aib.gif|left|200px]]<br /><applet load="2aib" size=" | + | [[Image:2aib.gif|left|200px]]<br /><applet load="2aib" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2aib, resolution 1.10Å" /> | caption="2aib, resolution 1.10Å" /> | ||
'''beta-cinnamomin in complex with ergosterol'''<br /> | '''beta-cinnamomin in complex with ergosterol'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of the elicitin beta-cinnamomin (beta-CIN) was | + | 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== | ||
| - | 2AIB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Phytophthora_cinnamomi Phytophthora cinnamomi] with ERG, MES and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 2AIB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Phytophthora_cinnamomi Phytophthora cinnamomi] with <scene name='pdbligand=ERG:'>ERG</scene>, <scene name='pdbligand=MES:'>MES</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AIB OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Archer, M.]] | [[Category: Archer, M.]] | ||
| - | [[Category: Baptista, R | + | [[Category: Baptista, R P.]] |
| - | [[Category: Carrondo, M | + | [[Category: Carrondo, M A.]] |
[[Category: Cravador, A.]] | [[Category: Cravador, A.]] | ||
| - | [[Category: Enguita, F | + | [[Category: Enguita, F J.]] |
[[Category: Martel, P.]] | [[Category: Martel, P.]] | ||
| - | [[Category: Melo, E | + | [[Category: Melo, E P.]] |
[[Category: Miranda, S.]] | [[Category: Miranda, S.]] | ||
| - | [[Category: Rodrigues, M | + | [[Category: Rodrigues, M L.]] |
[[Category: Sousa, N.]] | [[Category: Sousa, N.]] | ||
[[Category: Thomaz, M.]] | [[Category: Thomaz, M.]] | ||
| Line 32: | Line 32: | ||
[[Category: sterol carrier protein]] | [[Category: sterol carrier protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:27:41 2008'' |
Revision as of 14:27, 21 February 2008
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beta-cinnamomin in complex with ergosterol
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
2AIB is a Single protein structure of sequence from Phytophthora cinnamomi with , and as ligands. 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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