NMR assignments of cd-HO, a 24 kDa heme oxygenase from Corynebacterium diphtheria.
Biomol NMR Assign
; 1(1): 55-6, 2007 Jul.
Article
em En
| MEDLINE
| ID: mdl-19636825
ABSTRACT
We are employing a number of selective in vitro and in vivo methods including NMR to screen compounds that bind to heme oxygenases from pathogenic bacteria. We report the nearly complete HN, N, CO, Calpha and Cbeta chemical shift assignments of a 215-amino acid HO from Corynebacterium diphtheria in three forms, apo cd-HO-G135A, apo cd-HO and CO-bound ferrous holo cd-HO; these assignments will enable us to identify residues on cd-HO that are perturbed upon binding to selected compounds, and to help with the development of inhibitors specific to the bacterial proteins.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Proteínas de Bactérias
/
Corynebacterium diphtheriae
/
Heme Oxigenase (Desciclizante)
Idioma:
En
Revista:
Biomol NMR Assign
Assunto da revista:
BIOLOGIA MOLECULAR
/
MEDICINA NUCLEAR
Ano de publicação:
2007
Tipo de documento:
Article
País de afiliação:
Estados Unidos