Linked Life Data

12351633

Source:http://linkedlifedata.com/resource/pubmed/id/12351633

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2002-11-26
pubmed:abstractText
The antifungal protein AFP is a small polypeptide of 51 amino acid residues secreted by Aspergillus giganteus. Its potent activity against phytopathogenic fungi converts AFP in a promising tool in plant protection. However, no data have been reported regarding the mode of action of AFP. The three-dimensional structure of this protein, a small and compact beta barrel composed of five highly twisted antiparallel beta strands, displays the characteristic features of the oligonucleotide/oligosaccharide binding (OB fold) structural motif. A comparison of the structures of AFP and OB fold-containing proteins shows this structural similarity despite the absence of any significant sequence similarity. AFP, like most OB fold-containing proteins, binds nucleic acids. The protein promotes charge neutralization and condensation of DNA as demonstrated by electrophoretic mobility shift and ethidium bromide displacement assays. Nucleic acid produces quenching of the protein fluorescence emission. This nucleic acid interacting ability of AFP may be related to the antifungal activity of this small polypeptide.
pubmed:language
eng
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:author
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
46179-83
pubmed:dateRevised
2006-11-15
pubmed:articleTitle
The antifungal protein AFP of Aspergillus giganteus is an oligonucleotide/oligosaccharide binding (OB) fold-containing protein that produces condensation of DNA.
pubmed:affiliation
Departamento de Bioquimica y Biologia Molecular, Facultad de Quimica, Universidad Complutense, 28040 Madrid, Spain. alvaro@bbm1.ucm.es