2L2R
Helical hairpin structure of a novel antimicrobial peptide EcAMP1 from seeds of barnyard grass (Echinochloa crus-galli)
Summary for 2L2R
| Entry DOI | 10.2210/pdb2l2r/pdb |
| NMR Information | BMRB: 17152 |
| Descriptor | Antimicrobial peptide EcAMP1 (1 entity in total) |
| Functional Keywords | disulfide-stabilized helical hairpin, antifungal peptide, antimicrobial peptide, antimicrobial protein |
| Biological source | Echinochloa crus-galli (cockspur grass, barnyard grass, Echinochloa crus-galli (L.) P. Beauv.) |
| Total number of polymer chains | 1 |
| Total formula weight | 4288.78 |
| Authors | Nolde, S.B.,Barinov, N.A.,Balashova, T.A.,Arseniev, A.S.,Vassilevski, A.A.,Rogozhin, E.A.,Egorov, T.A.,Grishin, E.V. (deposition date: 2010-08-26, release date: 2011-05-11, Last modification date: 2024-10-09) |
| Primary citation | Nolde, S.B.,Vassilevski, A.A.,Rogozhin, E.A.,Barinov, N.A.,Balashova, T.A.,Samsonova, O.V.,Baranov, Y.V.,Feofanov, A.V.,Egorov, T.A.,Arseniev, A.S.,Grishin, E.V. Disulfide-stabilized Helical Hairpin Structure and Activity of a Novel Antifungal Peptide EcAMP1 from Seeds of Barnyard Grass (Echinochloa crus-galli). J.Biol.Chem., 286:25145-25153, 2011 Cited by PubMed Abstract: This study presents purification, activity characterization, and (1)H NMR study of the novel antifungal peptide EcAMP1 from kernels of barnyard grass Echinochloa crus-galli. The peptide adopts a disulfide-stabilized α-helical hairpin structure in aqueous solution and thus represents a novel fold among naturally occurring antimicrobial peptides. Micromolar concentrations of EcAMP1 were shown to inhibit growth of several fungal phytopathogens. Confocal microscopy revealed intensive EcAMP1 binding to the surface of fungal conidia followed by internalization and accumulation in the cytoplasm without disturbance of membrane integrity. Close spatial structure similarity between EcAMP1, the trypsin inhibitor VhTI from seeds of Veronica hederifolia, and some scorpion and cone snail toxins suggests natural elaboration of different functions on a common fold. PubMed: 21561864DOI: 10.1074/jbc.M110.200378 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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