1999
DOI: 10.1006/jmbi.1999.3163
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MiAMP1, a novel protein from Macadamia integrifolia adopts a greek key β-barrel fold unique amongst plant antimicrobial proteins 1 1Edited by P. E. Wright

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Cited by 59 publications
(51 citation statements)
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“…Three SSPs (Ecp20-1, Ecp20-2, and Ecp20-3) were consistently predicted to have structural homology to Alt a 1 (RCSB protein databank numbers 3V0R and 4AUD), an allergen protein with a b-barrel fold (Chruszcz et al 2012) from the broad host-range Dothideomycete fungal plant pathogen and saprophyte Alternaria alternata (Supplementary Table S2). Four SSPs (Ecp4, Ecp7, Ecp29 [CTR], and Ecp30) were consistently predicted to have structural homology to proteins with a b/g-crystallin fold, including the plant antimicrobial protein MiAMP1 from Macadamia integrifolia (1C01) (McManus et al 1999) and the yeast killer toxin WmKT from Williopsis mrakii (1WKT) (Antuch et al 1996). Three other SSPs (Ecp28-1, Ecp28-2, and Ecp28-3) were consistently predicted to have structural homology to one or both the a and b subunits of KP6 (1KP6 and 4GVB), a virus-encoded antifungal killer toxin with an a/b-sandwich fold secreted by the fungal corn smut pathogen Ustilago maydis (Allen et al 2013a;Li et al 1999).…”
Section: Resultsmentioning
confidence: 99%
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“…Three SSPs (Ecp20-1, Ecp20-2, and Ecp20-3) were consistently predicted to have structural homology to Alt a 1 (RCSB protein databank numbers 3V0R and 4AUD), an allergen protein with a b-barrel fold (Chruszcz et al 2012) from the broad host-range Dothideomycete fungal plant pathogen and saprophyte Alternaria alternata (Supplementary Table S2). Four SSPs (Ecp4, Ecp7, Ecp29 [CTR], and Ecp30) were consistently predicted to have structural homology to proteins with a b/g-crystallin fold, including the plant antimicrobial protein MiAMP1 from Macadamia integrifolia (1C01) (McManus et al 1999) and the yeast killer toxin WmKT from Williopsis mrakii (1WKT) (Antuch et al 1996). Three other SSPs (Ecp28-1, Ecp28-2, and Ecp28-3) were consistently predicted to have structural homology to one or both the a and b subunits of KP6 (1KP6 and 4GVB), a virus-encoded antifungal killer toxin with an a/b-sandwich fold secreted by the fungal corn smut pathogen Ustilago maydis (Allen et al 2013a;Li et al 1999).…”
Section: Resultsmentioning
confidence: 99%
“…In MiAMP1, all six Cys residues are known to form intramolecular disulphide bonds (Cys11-Cys65, Cys21-Cys76, and Cys23-Cys49) (McManus et al 1999). Inspection of the predicted Ecp4 structure, which was modeled using MiAMP1 as a template, suggests that two of the conserved Cys pairs, Cys16/Cys84 and Cys35/Cys67, form intramolecular disulphide bonds.…”
Section: Resultsmentioning
confidence: 99%
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“…The three-dimensional structure of b-barrelins is very similar to that of the fungal killer toxin HM-1, which interacts with b-(1,3)-glucans and blocks their synthesis (Kasahara et al 1994;McManus et al 1999). Regarding biotechnological applications, expression in canola of b-barrelins from macadamia and pine resulted in increased resistance to fungal pathogens (Kazan et al 2002;Verma et al 2012).…”
Section: B-barrelinsmentioning
confidence: 95%
“…4.1g). This protein, which is 76 amino acids long, forms a barrel of eight b-strands that includes three disulfide bonds (McManus et al 1999). Sequence conservation is high in the family and basic amino acids are abundant.…”
Section: B-barrelinsmentioning
confidence: 98%