Campylobacter jejuni fatty acid synthase II: structural and functional analysis of beta-hydroxyacyl-ACP dehydratase (FabZ).

Abstract:

:Fatty acid biosynthesis is crucial for all living cells. In contrast to higher organisms, bacteria use a type II fatty acid synthase (FAS II) composed of a series of individual proteins, making FAS II enzymes excellent targets for antibiotics discovery. The beta-hydroxyacyl-ACP dehydratase (FabZ) catalyzes an essential step in the FAS II pathway. Here, we report the structure of Campylobacter jejuni FabZ (CjFabZ), showing a hexamer both in crystals and solution, with each protomer adopting the characteristic hot dog fold. Together with biochemical analysis of CjFabZ, we define the first functional FAS II enzyme from this pathogen, and provide a framework for investigation on roles of FAS II in C. jejuni virulence.

authors

Kirkpatrick AS,Yokoyama T,Choi KJ,Yeo HJ

doi

10.1016/j.bbrc.2009.01.115

subject

Has Abstract

pub_date

2009-03-06 00:00:00

pages

407-12

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(09)00149-1

journal_volume

380

pub_type

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