The structure of E. coli β-galactosidase

E. coli β-galactosidase is a tetramer of four identical 1023-amino acid chains. Each chain consists of five domains, the third of which is an eight-stranded α / β barrel that comprises much of the active site. This site does, however, include elements from other domains and other subunits. The N-ter...

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Veröffentlicht in:	Comptes rendus. Biologies 2005-06, Vol.328 (6), p.549-556
1. Verfasser:	Matthews, Brian W.
Format:	Artikel
Sprache:	eng
Schlagworte:	Allolactose beta-Galactosidase - chemistry Binding Sites Enzyme Activation Escherichia coli - enzymology Hydrogen Bonding Lactose Magnesium - metabolism Models, Molecular Molecular Structure Tetramer α-complementation β-galactosidase
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