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| | ==NMR Solution Structure of plant defensin SlD26== | | ==NMR Solution Structure of plant defensin SlD26== |
| - | <StructureSection load='7jnn' size='340' side='right'caption='[[7jnn]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='7jnn' size='340' side='right'caption='[[7jnn]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[7jnn]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lycopersicon_esculentum Lycopersicon esculentum]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7JNN OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=7JNN FirstGlance]. <br> | + | <table><tr><td colspan='2'>Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7JNN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7JNN FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=7jnn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7jnn OCA], [http://pdbe.org/7jnn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=7jnn RCSB], [http://www.ebi.ac.uk/pdbsum/7jnn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=7jnn ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</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=7jnn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7jnn OCA], [https://pdbe.org/7jnn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7jnn RCSB], [https://www.ebi.ac.uk/pdbsum/7jnn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7jnn ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
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| | </div> | | </div> |
| | <div class="pdbe-citations 7jnn" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 7jnn" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Defensin 3D structures|Defensin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lycopersicon esculentum]]
| + | [[Category: Craik DJ]] |
| - | [[Category: Craik, D J]] | + | [[Category: Harvey PJ]] |
| - | [[Category: Harvey, P J]] | + | |
| - | [[Category: Antifungal protein]]
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| - | [[Category: Plant defensin]]
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| Structural highlights
Publication Abstract from PubMed
Plant defensins are best known for their antifungal activity and contribution to the plant immune system. The defining feature of plant defensins is their three-dimensional structure known as the cysteine stabilized alpha-beta motif. This protein fold is remarkably tolerant to sequence variation with only the eight cysteines that contribute to the stabilizing disulfide bonds absolutely conserved across the family. Mature defensins are typically 46-50 amino acids in length and are enriched in lysine and/or arginine residues. Examination of a database of approximately 1200 defensin sequences revealed a subset of defensin sequences that were extended in length and were enriched in histidine residues leading to their classification as histidine-rich defensins (HRDs). Using these initial HRD sequences as a query, a search of the available sequence databases identified over 750 HRDs in solanaceous plants and 20 in brassicas. Histidine residues are known to contribute to metal binding functions in proteins leading to the hypothesis that HRDs would have metal binding properties. A selection of the HRD sequences were recombinantly expressed and purified and their antifungal and metal binding activity was characterized. Of the four HRDs that were successfully expressed all displayed some level of metal binding and two of four had antifungal activity. Structural characterization of the other HRDs identified a novel pattern of disulfide linkages in one of the HRDs that is predicted to also occur in HRDs with similar cysteine spacing. Metal binding by HRDs represents a specialization of the plant defensin fold outside of antifungal activity.
Histidine-Rich Defensins from the Solanaceae and Brasicaceae Are Antifungal and Metal Binding Proteins.,Bleackley MR, Vasa S, Harvey PJ, Shafee TMA, Kerenga BK, Soares da Costa TP, Craik DJ, Lowe RGT, Anderson MA J Fungi (Basel). 2020 Aug 24;6(3). pii: jof6030145. doi: 10.3390/jof6030145. PMID:32847065[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Bleackley MR, Vasa S, Harvey PJ, Shafee TMA, Kerenga BK, Soares da Costa TP, Craik DJ, Lowe RGT, Anderson MA. Histidine-Rich Defensins from the Solanaceae and Brasicaceae Are Antifungal and Metal Binding Proteins. J Fungi (Basel). 2020 Aug 24;6(3). pii: jof6030145. doi: 10.3390/jof6030145. PMID:32847065 doi:http://dx.doi.org/10.3390/jof6030145
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