Expression, purification, crystallization and preliminary crystallographic analysis of SpaA, a major pilin from Corynebacterium diphtheriae.
Acta Crystallogr Sect F Struct Biol Cryst Commun
; 65(Pt 8): 802-4, 2009 Aug 01.
Article
em En
| MEDLINE
| ID: mdl-19652344
ABSTRACT
Bacterial pili are cell-surface organelles that are critically involved in adhesion to host cells, leading to the colonization of host tissues and the establishment of infections. Whereas the pili of Gram-negative bacteria have been extensively studied, those of Gram-positive bacteria came to light only recently after the discovery and characterization of Corynebacterium diphtheriae pili. These newly discovered pili are formed by the covalent polymerization of pilin subunits catalyzed by sortase enzymes, making them fundamentally different from the noncovalent pilin assemblies of Gram-negative bacteria. Here, the expression, crystallization and preliminary crystallographic analysis of SpaA, which forms the shaft of one of the three types of pili expressed by C. diphtheriae, are reported. SpaA(53-486) crystals diffracted to 1.6 A resolution and belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 34.9, b = 64.1, c = 198.7 A, alpha = beta = gamma = 90 degrees .
Texto completo:
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Base de dados:
MEDLINE
Assunto principal:
Proteínas de Bactérias
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Corynebacterium diphtheriae
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Proteínas de Fímbrias
Idioma:
En
Revista:
Acta Crystallogr Sect F Struct Biol Cryst Commun
Ano de publicação:
2009
Tipo de documento:
Article
País de afiliação:
Nova Zelândia