Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3D6X

Crystal structure of Campylobacter jejuni FabZ

Summary for 3D6X
Entry DOI10.2210/pdb3d6x/pdb
Descriptor(3R)-hydroxymyristoyl-[acyl-carrier-protein] dehydratase (2 entities in total)
Functional Keywordsfabz, hot dog fold, dehydratase, campylobacter jejuni, lipid a biosynthesis, lipid synthesis, lyase
Biological sourceCampylobacter jejuni subsp. jejuni 81-176
Cellular locationCytoplasm (By similarity): A1VXZ7
Total number of polymer chains6
Total formula weight101018.41
Authors
Yokoyama, T.,Yeo, H.J. (deposition date: 2008-05-20, release date: 2009-05-05, Last modification date: 2024-11-06)
Primary citationKirkpatrick, 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: 19280690
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.59 Å)
Structure validation

227344

PDB entries from 2024-11-13

PDB statisticsPDBj update infoContact PDBjnumon