7JNN
NMR Solution Structure of plant defensin SlD26
Summary for 7JNN
| Entry DOI | 10.2210/pdb7jnn/pdb |
| NMR Information | BMRB: 30784 |
| Descriptor | SlD26 plant defensin (1 entity in total) |
| Functional Keywords | plant defensin, antifungal protein |
| Biological source | Solanum lycopersicum (Tomato) |
| Total number of polymer chains | 1 |
| Total formula weight | 5444.24 |
| Authors | Harvey, P.J.,Craik, D.J. (deposition date: 2020-08-04, release date: 2020-09-09, Last modification date: 2024-11-06) |
| Primary citation | Bleackley, M.R.,Vasa, S.,Harvey, P.J.,Shafee, T.M.A.,Kerenga, B.K.,Soares da Costa, T.P.,Craik, D.J.,Lowe, R.G.T.,Anderson, M.A. Histidine-Rich Defensins from the Solanaceae and Brasicaceae Are Antifungal and Metal Binding Proteins. J Fungi (Basel), 6:-, 2020 Cited by PubMed Abstract: 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. PubMed: 32847065DOI: 10.3390/jof6030145 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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