4ab0

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{{STRUCTURE_4ab0| PDB=4ab0 | SCENE= }}
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==X-ray crystal structure of Nicotiana alata defensin NaD1==
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===X-ray crystal structure of Nicotiana alata defensin NaD1===
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<StructureSection load='4ab0' size='340' side='right' caption='[[4ab0]], [[Resolution|resolution]] 1.64&Aring;' scene=''>
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{{ABSTRACT_PUBMED_22511788}}
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4ab0]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Nicotiana_alata Nicotiana alata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AB0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4AB0 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4aaz|4aaz]]</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ab0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ab0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ab0 RCSB], [http://www.ebi.ac.uk/pdbsum/4ab0 PDBsum]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The plant defensin, NaD1, from the flowers of Nicotiana alata, is a member of a family of cationic peptides that displays growth inhibitory activity against several filamentous fungi, including Fusarium oxysporum. The antifungal activity of NaD1 has been attributed to its ability to permeabilize membranes; however, the molecular basis of this function remains poorly defined. In this study, we have solved the structure of NaD1 from two crystal forms to high resolution (1.4 and 1.58 A, respectively), both of which contain NaD1 in a dimeric configuration. Using protein cross-linking experiments as well as small angle x-ray scattering analysis and analytical ultracentrifugation, we show that NaD1 forms dimers in solution. The structural studies identified Lys(4) as critical in formation of the NaD1 dimer. This was confirmed by site-directed mutagenesis of Lys(4) that resulted in substantially reduced dimer formation. Significantly, the reduced ability of the Lys(4) mutant to dimerize correlated with diminished antifungal activity. These data demonstrate the importance of dimerization in NaD1 function and have implications for the use of defensins in agribiotechnology applications such as enhancing plant crop protection against fungal pathogens.
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==About this Structure==
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Dimerization of Plant Defensin NaD1 Enhances Its Antifungal Activity.,Lay FT, Mills GD, Poon IK, Cowieson NP, Kirby N, Baxter AA, van der Weerden NL, Dogovski C, Perugini MA, Anderson MA, Kvansakul M, Hulett MD J Biol Chem. 2012 Jun 8;287(24):19961-72. Epub 2012 Apr 17. PMID:22511788<ref>PMID:22511788</ref>
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[[4ab0]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Nicotiana_alata Nicotiana alata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AB0 OCA].
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
==See Also==
==See Also==
*[[Defensin|Defensin]]
*[[Defensin|Defensin]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:022511788</ref><references group="xtra"/>
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__TOC__
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</StructureSection>
[[Category: Nicotiana alata]]
[[Category: Nicotiana alata]]
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[[Category: Hulett, M D.]]
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[[Category: Hulett, M D]]
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[[Category: Kvansakul, M.]]
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[[Category: Kvansakul, M]]
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[[Category: Lay, F T.]]
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[[Category: Lay, F T]]
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[[Category: Mills, G D.]]
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[[Category: Mills, G D]]
[[Category: Antimicrobial protein]]
[[Category: Antimicrobial protein]]
[[Category: Innate immunity]]
[[Category: Innate immunity]]

Revision as of 08:41, 18 December 2014

X-ray crystal structure of Nicotiana alata defensin NaD1

4ab0, resolution 1.64Å

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