4K22
Structure of the C-terminal truncated form of E.Coli C5-hydroxylase UBII involved in ubiquinone (Q8) biosynthesis
Summary for 4K22
| Entry DOI | 10.2210/pdb4k22/pdb |
| Descriptor | Protein VisC, GLYCEROL, CHLORIDE ION, ... (5 entities in total) |
| Functional Keywords | rossmann fold, hydroxylase, oxidoreductase |
| Biological source | Escherichia coli |
| Total number of polymer chains | 2 |
| Total formula weight | 81610.30 |
| Authors | Pecqueur, L.,Lombard, M.,Golinelli-pimpaneau, B.,Fontecave, M. (deposition date: 2013-04-07, release date: 2013-05-29, Last modification date: 2024-03-20) |
| Primary citation | Chehade, M.H.,Loiseau, L.,Lombard, M.,Pecqueur, L.,Ismail, A.,Smadja, M.,Golinelli-Pimpaneau, B.,Mellot-Draznieks, C.,Hamelin, O.,Aussel, L.,Kieffer-Jaquinod, S.,Labessan, N.,Barras, F.,Fontecave, M.,Pierrel, F. ubiI, a New Gene in Escherichia coli Coenzyme Q Biosynthesis, Is Involved in Aerobic C5-hydroxylation. J.Biol.Chem., 288:20085-20092, 2013 Cited by PubMed Abstract: Coenzyme Q (ubiquinone or Q) is a redox-active lipid found in organisms ranging from bacteria to mammals in which it plays a crucial role in energy-generating processes. Q biosynthesis is a complex pathway that involves multiple proteins. In this work, we show that the uncharacterized conserved visC gene is involved in Q biosynthesis in Escherichia coli, and we have renamed it ubiI. Based on genetic and biochemical experiments, we establish that the UbiI protein functions in the C5-hydroxylation reaction. A strain deficient in ubiI has a low level of Q and accumulates a compound derived from the Q biosynthetic pathway, which we purified and characterized. We also demonstrate that UbiI is only implicated in aerobic Q biosynthesis and that an alternative enzyme catalyzes the C5-hydroxylation reaction in the absence of oxygen. We have solved the crystal structure of a truncated form of UbiI. This structure shares many features with the canonical FAD-dependent para-hydroxybenzoate hydroxylase and represents the first structural characterization of a monooxygenase involved in Q biosynthesis. Site-directed mutagenesis confirms that residues of the flavin binding pocket of UbiI are important for activity. With our identification of UbiI, the three monooxygenases necessary for aerobic Q biosynthesis in E. coli are known. PubMed: 23709220DOI: 10.1074/jbc.M113.480368 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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