Structure-Function Analysis of the Extended Conformation of a Polyketide Synthase Module.
J Am Chem Soc
; 140(21): 6518-6521, 2018 05 30.
Article
em En
| MEDLINE
| ID: mdl-29762030
ABSTRACT
Catalytic modules of assembly-line polyketide synthases (PKSs) have previously been observed in two very different conformations-an "extended" architecture and an "arch-shaped" architecture-although the catalytic relevance of neither has been directly established. By the use of a fully human naïve antigen-binding fragment (Fab) library, a high-affinity antibody was identified that bound to the extended conformation of a PKS module, as verified by X-ray crystallography and tandem size-exclusion chromatography-small-angle X-ray scattering (SEC-SAXS). Kinetic analysis proved that this antibody-stabilized module conformation was fully competent for catalysis of intermodular polyketide chain translocation as well as intramodular polyketide chain elongation and functional group modification of a growing polyketide chain. Thus, the extended conformation of a PKS module is fully competent for all of its essential catalytic functions.
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1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Policetídeo Sintases
Limite:
Humans
Idioma:
En
Revista:
J Am Chem Soc
Ano de publicação:
2018
Tipo de documento:
Article