The active site protonation states of perdeuterated Toho-1 ß-lactamase determined by neutron diffraction support a role for Glu166 as the general base in acylation.
FEBS Lett
; 585(2): 364-8, 2011 Jan 21.
Article
em En
| MEDLINE
| ID: mdl-21168411
ABSTRACT
Room temperature neutron diffraction data of the fully perdeuterated Toho-1 R274N/R276N double mutant ß-lactamase in the apo form were used to visualize deuterium atoms within the active site of the enzyme. This perdeuterated neutron structure of the Toho-1 R274N/R276N reveals the clearest picture yet of the ground-state active site protonation states and the complete hydrogen-bonding network in a ß-lactamase enzyme. The ground-state active site protonation states detailed in this neutron diffraction study are consistent with previous high-resolution X-ray studies that support the role of Glu166 as the general base during the acylation reaction in the class A ß-lactamase reaction pathway.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Beta-Lactamases
/
Acilação
/
Difração de Nêutrons
/
Deutério
Idioma:
En
Ano de publicação:
2011
Tipo de documento:
Article