3D6X
Crystal structure of Campylobacter jejuni FabZ
Summary for 3D6X
Entry DOI | 10.2210/pdb3d6x/pdb |
Descriptor | (3R)-hydroxymyristoyl-[acyl-carrier-protein] dehydratase (2 entities in total) |
Functional Keywords | fabz, hot dog fold, dehydratase, campylobacter jejuni, lipid a biosynthesis, lipid synthesis, lyase |
Biological source | Campylobacter jejuni subsp. jejuni 81-176 |
Cellular location | Cytoplasm (By similarity): A1VXZ7 |
Total number of polymer chains | 6 |
Total formula weight | 101018.41 |
Authors | Yokoyama, T.,Yeo, H.J. (deposition date: 2008-05-20, release date: 2009-05-05, Last modification date: 2024-11-06) |
Primary citation | Kirkpatrick, A.S.,Yokoyama, T.,Choi, K.J.,Yeo, H.J. Campylobacter jejuni fatty acid synthase II: structural and functional analysis of beta-hydroxyacyl-ACP dehydratase (FabZ). Biochem.Biophys.Res.Commun., 380:407-412, 2009 Cited by PubMed 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. PubMed: 19280690PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.59 Å) |
Structure validation
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