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Gating mechanism of elongating β-ketoacyl-ACP synthases.

Abstract：

:Carbon-carbon bond forming reactions are essential transformations in natural product biosynthesis. During de novo fatty acid and polyketide biosynthesis, β-ketoacyl-acyl carrier protein (ACP) synthases (KS), catalyze this process via a decarboxylative Claisen-like condensation reaction. KSs must recognize multiple chemically distinct ACPs and choreograph a ping-pong mechanism, often in an iterative fashion. Here, we report crystal structures of substrate mimetic bearing ACPs in complex with the elongating KSs from Escherichia coli, FabF and FabB, in order to better understand the stereochemical features governing substrate discrimination by KSs. Complemented by molecular dynamics (MD) simulations and mutagenesis studies, these structures reveal conformational states accessed during KS catalysis. These data taken together support a gating mechanism that regulates acyl-ACP binding and substrate delivery to the KS active site. Two active site loops undergo large conformational excursions during this dynamic gating mechanism and are likely evolutionarily conserved features in elongating KSs.

journal_name

Nat Commun

journal_title

Nature communications

authors

Mindrebo JT,Patel A,Kim WE,Davis TD,Chen A,Bartholow TG,La Clair JJ,McCammon JA,Noel JP,Burkart MD

doi

10.1038/s41467-020-15455-x

subject

Has Abstract

pub_date

2020-04-07 00:00:00

pages

1727

issue

1

issn

2041-1723

pii

10.1038/s41467-020-15455-x

journal_volume

11

pub_type

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