This domain includes plant antimicrobial peptides [ (PUBMED:1527010) (PUBMED:21561864) ]. They adopt an alpha-helical hairpin fold stabilised by two disulphide bonds [ (PUBMED:21561864) ].
There are 256 Antimicrobial21 domains in 55 proteins in SMART's nrdb database.
Click on the following links for more information.
Evolution (species in which this domain is found)
Taxonomic distribution of proteins containing Antimicrobial21 domain.
This tree includes only several representative species. The complete taxonomic breakdown of all proteins with Antimicrobial21 domain is also avaliable.
Click on the protein counts, or double click on taxonomic names to display all proteins containing Antimicrobial21 domain in the selected taxonomic class.
Literature (relevant references for this domain)
Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.
Disulfide-stabilized helical hairpin structure and activity of a novel antifungalpeptide EcAMP1 from seeds of barnyard grass (Echinochloa crus-galli).
J Biol Chem. 2011; 286: 25145-53
Display abstract
This study presents purification, activity characterization, and (1)H NMR studyof the novel antifungal peptide EcAMP1 from kernels of barnyard grass Echinochloacrus-galli. The peptide adopts a disulfide-stabilized alpha-helical hairpinstructure in aqueous solution and thus represents a novel fold among naturallyoccurring 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 byinternalization and accumulation in the cytoplasm without disturbance of membraneintegrity. Close spatial structure similarity between EcAMP1, the trypsininhibitor VhTI from seeds of Veronica hederifolia, and some scorpion and conesnail toxins suggests natural elaboration of different functions on a commonfold.
Purification and characterization of a novel antimicrobial peptide from maize(Zea mays L.) kernels.
J Biol Chem. 1992; 267: 18814-20
Display abstract
Several small, acid-soluble, basic peptides with anti-microbial properties havebeen isolated from maize (inbred B73) kernels. One of these peptides (MBP-1) has been purified to homogeneity and characterized. The peptide has a molecularweight of 4127.08 as determined by plasma desorption mass spectroscopy, has nofree cysteines, and is predominantly alpha-helical as determined by circulardichroism. The primary sequence of the peptide (33 residues) has been determined by Edman degradation and shows no homology to the thionins, a group ofcysteine-rich peptides found in some cereals including wheat, barley, andsorghum, as well as several dicot species. Like the thionins, however, MBP-1 has been found to have antimicrobial properties in vitro. MBP-1 inhibits sporegermination or hyphal elongation of several plant pathogenic fungi, including twoseed pathogens of maize (Fusarium moniliforme Sheld. and Fusarium graminearum(Gibberella zeae (Schw.) Petsch)), and several bacteria, including a bacterialpathogen of maize (Clavibacter michiganense ssp. nebraskense). A synthetic MBP-1 peptide, air-oxidized and purified by reverse phase chromatography, was equallyantifungal as compared with the naturally occurring peptide.
