4OD4

Apo structure of a UbiA homolog from Aeropyrum pernix K1

Summary for 4OD4

• Entry DOI: 10.2210/pdb4od4/pdb
• Related: 4OD5
• Descriptor: 4-hydroxybenzoate octaprenyltransferase (1 entity in total)
• Functional Keywords: all alpha helical, intramembrane aromatic prenyltransferase, membrane, transferase
• Biological source: Aeropyrum pernix
• Total number of polymer chains: 6
• Total formula weight: 191018.77

Authors

Li, W.,Cheng, W. (deposition date: 2014-01-09, release date: 2014-03-19, Last modification date: 2024-02-28)

Primary citation

Cheng, W.,Li, W.
Structural insights into ubiquinone biosynthesis in membranes.
Science, 343:878-881, 2014

PubMed Abstract: 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.

PubMed: 24558159
DOI: 10.1126/science.1246774

Experimental method

X-RAY DIFFRACTION (3.301 Å)