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.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Kirkpatrick AS,Yokoyama T,Choi KJ,Yeo HJdoi
10.1016/j.bbrc.2009.01.115subject
Has Abstractpub_date
2009-03-06 00:00:00pages
407-12issue
2eissn
0006-291Xissn
1090-2104pii
S0006-291X(09)00149-1journal_volume
380pub_type
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