4OD5: Substrate-bound Structure Of A Ubia Homolog From Aeropyrum Pernix K1

Biosynthesis of ubiquinones requires the intramembrane UbiA enzyme, an archetypal member of a superfamily of prenyltransferases that generates lipophilic aromatic compounds. Mutations in eukaryotic superfamily members have been linked to cardiovascular degeneration and Parkinson's disease. To understand how quinones are produced within membranes, we report the crystal structures of an archaeal UbiA in its apo and substrate-bound states at 3.3 and 3.6 angstrom resolution, respectively. The structures reveal nine transmembrane helices and an extramembrane cap domain that surround a large central cavity containing the active site. To facilitate the catalysis inside membranes, UbiA has an unusual active site that opens laterally to the lipid bilayer. Our studies illuminate general mechanisms for substrate recognition and catalysis in the UbiA superfamily and rationalize disease-related mutations in humans.
PDB ID: 4OD5Download
MMDB ID: 118485
PDB Deposition Date: 2014/1/10
Updated in MMDB: 2014/03
Experimental Method:
x-ray diffraction
Resolution: 3.56  Å
Source Organism:
Similar Structures:
Biological Unit for 4OD5: monomeric; determined by author and by software (PISA)
Molecular Components in 4OD5
Label Count Molecule
Protein (1 molecule)
4-hydroxybenzoate Octaprenyltransferase
Molecule annotation
Chemicals (3 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB