Structure of apo-glyceraldehyde-3-phosphate dehydrogenase from Palinurus versicolor.
J Struct Biol
; 130(1): 1-9, 2000 May.
Article
em En
| MEDLINE
| ID: mdl-10806086
ABSTRACT
d-Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) shows cooperative properties for binding coenzymes. The structure of apo-GAPDH from Palinurus versicolor has been solved at 2.0 A resolution by X-ray crystallography. The final model gives a crystallographic R factor of 0.178 in the resolution range 8 to 2 A. The structural comparison with holo-GAPDH from the same species reveals a conformational change induced by coenzyme binding similar to that observed in Bacillus stearothermophilus GAPDH but to a lesser extent. The differences in magnitude during the apo-holo transition between these two enzymes were analyzed with respect to the change of the amino acid composition in the coenzyme binding pocket. In the crystalline state of apo-GAPDH, the overall structures of the subunits are similar to each other; however, significant differences in temperature factors and minor differences in domain rotation upon coenzyme binding were observed for different subunits. These structural features are discussed in relation to the environmental asymmetry of crystallographically independent subunits.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Gliceraldeído-3-Fosfato Desidrogenases
/
Nephropidae
Tipo de estudo:
Prognostic_studies
Limite:
Animals
Idioma:
En
Revista:
J Struct Biol
Assunto da revista:
BIOLOGIA MOLECULAR
Ano de publicação:
2000
Tipo de documento:
Article