Antimicrobial peptide CRAMP (16-33) stalls bacterial cytokinesis by inhibiting FtsZ assembly.
Biochemistry
; 53(41): 6426-9, 2014 Oct 21.
Article
em En
| MEDLINE
| ID: mdl-25294259
ABSTRACT
A cathelin-related antimicrobial peptide (CRAMP) of 37 amino acid residues is thought to regulate innate immunity and provide a host defense mechanism in mammals. Here, a part of the CRAMP peptide, CRAMP (16-33) (GEKLKKIGQKIKNFFQKL), was found to bind to FtsZ and to inhibit the assembly and GTPase activity of FtsZ in vitro. A computational analysis indicated that CRAMP (16-33) binds in the cavity of the T7 loop of FtsZ. Both hydrophobic and ionic interactions were involved in the binding interactions. Further, CRAMP (16-33) inhibited the formation of the FtsZ ring in bacteria, indicating that it inhibited bacterial cell division by inhibiting FtsZ assembly.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Fragmentos de Peptídeos
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Proteínas de Bactérias
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Modelos Moleculares
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Peptídeos Catiônicos Antimicrobianos
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Proteínas do Citoesqueleto
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Citocinese
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Inibidores Enzimáticos
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Catelicidinas
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Antibacterianos
Idioma:
En
Revista:
Biochemistry
Ano de publicação:
2014
Tipo de documento:
Article
País de afiliação:
Índia