Crystallization of a nonclassical Kazal-type Carcinoscorpius rotundicauda serine protease inhibitor, CrSPI-1, complexed with subtilisin.
Acta Crystallogr Sect F Struct Biol Cryst Commun
; 65(Pt 5): 533-5, 2009 May 01.
Article
em En
| MEDLINE
| ID: mdl-19407396
ABSTRACT
Serine proteases play a major role in host-pathogen interactions. The innate immune system is known to respond to invading pathogens in a nonspecific manner. The serine protease cascade is an essential component of the innate immune system of the horseshoe crab. The serine protease inhibitor CrSPI isoform 1 (CrSPI-1), a unique nonclassical Kazal-type inhibitor of molecular weight 9.3 kDa, was identified from the hepatopancreas of the horseshoe crab Carcinoscorpius rotundicauda. It potently inhibits subtilisin and constitutes a powerful innate immune defence against invading microbes. Here, the cloning, expression, purification and cocrystallization of CrSPI-1 with subtilisin are reported. The crystals diffracted to 2.6 A resolution and belonged to space group P2(1), with unit-cell parameters a = 73.8, b = 65.0, c = 111.9 A, beta = 95.4 degrees . The Matthews coefficient (V(M) = 2.64 A(3) Da(-1), corresponding to 53% solvent content) and analysis of the preliminary structure solution indicated the presence of one heterotrimer (12 ratio of CrSPI-1subtilisin) and one free subtilisin molecule in the asymmetric unit.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Inibidores de Serina Proteinase
/
Subtilisina
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Caranguejos Ferradura
Limite:
Animals
Idioma:
En
Revista:
Acta Crystallogr Sect F Struct Biol Cryst Commun
Ano de publicação:
2009
Tipo de documento:
Article
País de afiliação:
Singapura