Functional analysis of substrate and cofactor complex structures of a thymidylate synthase-complementing protein.
Structure
; 11(6): 677-90, 2003 Jun.
Article
em En
| MEDLINE
| ID: mdl-12791256
ABSTRACT
Like thymidylate synthase (TS) in eukaryotes, the thymidylate synthase-complementing proteins (TSCPs) are mandatory for cell survival of many prokaryotes in the absence of external sources of thymidylate. Details of the mechanism of this novel family of enzymes are unknown. Here, we report the structural and functional analysis of a TSCP from Thermotoga maritima and its complexes with substrate, analogs, and cofactor. The structures presented here provide a basis for rationalizing the TSCP catalysis and reveal the possibility of the design of an inhibitor. We have identified a new helix-loop-strand FAD binding motif characteristic of the enzymes in the TSCP family. The presence of a hydrophobic core with residues conserved among the TSCP family suggests a common overall fold.
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Base de dados:
MEDLINE
Assunto principal:
Timidilato Sintase
/
Proteínas de Bactérias
/
Estrutura Terciária de Proteína
/
Thermotoga maritima
Tipo de estudo:
Prognostic_studies
Idioma:
En
Ano de publicação:
2003
Tipo de documento:
Article