Crystal structures of thiamine monophosphate kinase from Acinetobacter baumannii in complex with substrates and products.
Sci Rep
; 9(1): 4392, 2019 03 13.
Article
em En
| MEDLINE
| ID: mdl-30867460
ABSTRACT
Thiamine monophosphate kinase (ThiL) catalyzes the last step of thiamine pyrophosphate (TPP) synthesis, the ATP-dependent phosphorylation of thiamine monophosphate (TMP) to thiamine pyrophosphate. We solved the structure of ThiL from the human pathogen A. baumanii in complex with a pair of substrates TMP and a non-hydrolyzable adenosine triphosphate analog, and in complex with a pair of products TPP and adenosine diphosphate. High resolution of the data and anomalous diffraction allows for a detailed description of the binding mode of substrates and products, and their metal environment. The structures further support a previously proposed in-line attack reaction mechanism and show a distinct variability of metal content of the active site.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Fosfotransferases (Aceptor do Grupo Fosfato)
/
Acinetobacter baumannii
Idioma:
En
Ano de publicação:
2019
Tipo de documento:
Article