Insights into trehalose synthesis provided by the structure of the retaining glucosyltransferase OtsA.
Chem Biol
; 9(12): 1337-46, 2002 Dec.
Article
en En
| MEDLINE
| ID: mdl-12498887
ABSTRACT
Trehalose is a nonreducing disaccharide that plays a major role in many organisms, most notably in survival and stress responses. In Mycobacterium tuberculosis, it plays a central role as the carbohydrate core of numerous immunogenic glycolipids including "cord factor" (trehalose 6,6'-dimycolate). The classical pathway for trehalose synthesis involves the condensation of UDP-glucose and glucose-6-phosphate to afford trehalose-6-phosphate, catalyzed by the retaining glycosyltransferase OtsA. The configurations of two anomeric positions are set simultaneously, resulting in the formation of a double glycoside. The three-dimensional structure of the Escherichia coli OtsA, in complex with both UDP and glucose-6-phosphate, reveals the active site at the interface of two beta/alpha/beta domains. The overall structure and the intimate details of the catalytic machinery reveal a striking similarity to glycogen phosphorylase, indicating a strong evolutionary link and suggesting a common catalytic mechanism.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Trehalosa
/
Glucosiltransferasas
Tipo de estudio:
Prognostic_studies
Idioma:
En
Revista:
Chem Biol
Asunto de la revista:
BIOLOGIA
/
BIOQUIMICA
/
QUIMICA
Año:
2002
Tipo del documento:
Article
País de afiliación:
Reino Unido