2a8f: Difference between revisions
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< | ==beta-cinnamomin after sterol removal== | ||
<StructureSection load='2a8f' size='340' side='right'caption='[[2a8f]], [[Resolution|resolution]] 1.35Å' scene=''> | |||
You may | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2a8f]] is a 2 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2A8F FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.35Å</td></tr> | |||
-- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2a8f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a8f OCA], [https://pdbe.org/2a8f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2a8f RCSB], [https://www.ebi.ac.uk/pdbsum/2a8f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2a8f ProSAT]</span></td></tr> | ||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/ELIB_PHYCI ELIB_PHYCI] Induces local and distal defense responses (incompatible hypersensitive reaction) in plants from the solanaceae and cruciferae families. Elicits leaf necrosis and causes the accumulation of pathogenesis-related proteins. Might interact with the lipidic molecules of the plasma membrane. Elicitins are able to load, carry, and transfer sterols between membranes. | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a8/2a8f_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2a8f ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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<ref>PMID:16249127</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2a8f" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
< | |||
[[Category: Phytophthora cinnamomi]] | [[Category: Phytophthora cinnamomi]] | ||
[[Category: Archer | [[Category: Archer M]] | ||
[[Category: Baptista | [[Category: Baptista RP]] | ||
[[Category: Carrondo | [[Category: Carrondo MA]] | ||
[[Category: Cravador | [[Category: Cravador A]] | ||
[[Category: Enguita | [[Category: Enguita FJ]] | ||
[[Category: Martel | [[Category: Martel P]] | ||
[[Category: Melo | [[Category: Melo EP]] | ||
[[Category: Miranda | [[Category: Miranda S]] | ||
[[Category: Rodrigues | [[Category: Rodrigues ML]] | ||
[[Category: Sousa | [[Category: Sousa N]] | ||
[[Category: Thomaz | [[Category: Thomaz M]] | ||
Latest revision as of 10:33, 9 October 2024
beta-cinnamomin after sterol removalbeta-cinnamomin after sterol removal
Structural highlights
FunctionELIB_PHYCI Induces local and distal defense responses (incompatible hypersensitive reaction) in plants from the solanaceae and cruciferae families. Elicits leaf necrosis and causes the accumulation of pathogenesis-related proteins. Might interact with the lipidic molecules of the plasma membrane. Elicitins are able to load, carry, and transfer sterols between membranes. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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