Modular polyketide synthase contains two reaction chambers that operate asynchronously.
Science
; 374(6568): 723-729, 2021 Nov 05.
Article
en En
| MEDLINE
| ID: mdl-34735234
ABSTRACT
Type I modular polyketide synthases are homodimeric multidomain assembly line enzymes that synthesize a variety of polyketide natural products by performing polyketide chain extension and ß-keto group modification reactions. We determined the 2.4-angstrom-resolution x-ray crystal structure and the 3.1-angstrom-resolution cryoelectron microscopy structure of the Lsd14 polyketide synthase, stalled at the transacylation and condensation steps, respectively. These structures revealed how the constituent domains are positioned relative to each other, how they rearrange depending on the step in the reaction cycle, and the specific interactions formed between the domains. Like the evolutionarily related mammalian fatty acid synthase, Lsd14 contains two reaction chambers, but only one chamber in Lsd14 has the full complement of catalytic domains, indicating that only one chamber produces the polyketide product at any given time.
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Streptomyces
/
Sintasas Poliquetidas
Idioma:
En
Revista:
Science
Año:
2021
Tipo del documento:
Article
País de afiliación:
Estados Unidos