Crystallization and preliminary X-ray diffraction analysis of the peptidylprolyl isomerase Par27 of Bordetella pertussis.
Acta Crystallogr Sect F Struct Biol Cryst Commun
; 64(Pt 9): 809-12, 2008 Sep 01.
Article
em En
| MEDLINE
| ID: mdl-18765910
ABSTRACT
Proteins with both peptidylprolyl isomerase (PPIase) and chaperone activities play a crucial role in protein folding in the periplasm of Gram-negative bacteria. Few such proteins have been structurally characterized and to date only the crystal structure of SurA from Escherichia coli has been reported. Par27, the prototype of a new group of parvulins, has recently been identified. Par27 exhibits both chaperone and PPIase activities in vitro and is the first identified parvulin protein that forms dimers in solution. Par27 has been expressed in E. coli. The protein was purified using affinity and gel-filtration chromatographic techniques and crystallized in two different crystal forms. Form A, which belongs to space group P2 (unit-cell parameters a = 42.2, b = 142.8, c = 56.0 A, beta = 95.1 degrees ), diffracts to 2.8 A resolution, while form B, which belongs to space group C222 (unit-cell parameters a = 54.6, b = 214.1, c = 57.8 A), diffracts to 2.2 A resolution. Preliminary diffraction data analysis agreed with the presence of one monomer in the asymmetric unit of the orthorhombic crystal form and two in the monoclinic form.
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Base de dados:
MEDLINE
Assunto principal:
Bordetella pertussis
/
Proteínas de Transporte
/
Peptidilprolil Isomerase
Idioma:
En
Revista:
Acta Crystallogr Sect F Struct Biol Cryst Commun
Ano de publicação:
2008
Tipo de documento:
Article
País de afiliação:
França