Campylobacter jejuni fatty acid synthase II: structural and functional analysis of beta-hydroxyacyl-ACP dehydratase (FabZ).
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.
Kirkpatrick
Andrew S
AS
Department of Biology and Biochemistry, University of Houston, 4800 Calhoun, Houston, TX 77204, USA.
Yokoyama
Takeshi
T
Choi
Kyoung-Jae
KJ
Yeo
Hye-Jeong
HJ
D000595:Amino Acid Sequence; D016123:Campylobacter jejuni / Q000201:enzymology*; D002384:Catalysis; D018360:Crystallography, X-Ray; D054889:Fatty Acid Synthase, Type II / Q000737:chemistry* / Q000378:metabolism*; D005227:Fatty Acids / Q000096:biosynthesis; D006836:Hydro-Lyases / Q000737:chemistry* / Q000378:metabolism*; D008969:Molecular Sequence Data; D011487:Protein Conformation
D005227:Fatty Acids; D006836:Hydro-Lyases; C036180:beta-hydroxyacyl-(acyl-carrier-protein)dehydrase; D054889:Fatty Acid Synthase, Type II