PMID:18455185
| Citation |
Kim, IK, Yim, HS, Kim, MK, Kim, DW, Kim, YM, Cha, SS and Kang, SO (2008) Crystal structure of a new type of NADPH-dependent quinone oxidoreductase (QOR2) from Escherichia coli. J. Mol. Biol. 379:372-84 |
|---|---|
| Abstract |
Escherichia coli QOR2 [NAD(P)H-dependent quinone oxidoreductase; a ytfG gene product], which catalyzes two-electron reduction of methyl-1,4-benzoquinone, is a new type of quinone-reducing enzyme with distinct primary sequence and oligomeric conformation from previously known quinone oxidoreductases. The crystal structures of native QOR2 and the QOR2-NADPH (nicotinamide adenine dinucleotide phosphate, reduced form) complex reveal that QOR2 consists of two domains (N-domain and C-domain) resembling those of NmrA, a negative transcriptional regulator that belongs to the short-chain dehydrogenase/reductase family. The N-domain, which adopts the Rossmann fold, provides a platform for NADPH binding, whereas the C-domain, which contains a hydrophobic pocket connected to the NADPH-binding site, appears to play important roles in substrate binding. Asn143 near the NADPH-binding site has been identified to be involved in substrate binding and catalysis from structural and mutational analyses. Moreover, compared with wild-type strain, the qor2-overexpressing strain shows growth retardation and remarkable decrease in several enzymes involved in carbon metabolism, suggesting that QOR2 could play some physiological roles in addition to quinone reduction. |
| Links |
PubMed Online version:10.1016/j.jmb.2008.04.003 |
| Keywords |
Amino Acid Sequence; Crystallography, X-Ray; DNA Mutational Analysis; Escherichia coli/enzymology; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Fungal Proteins/chemistry; Fungal Proteins/genetics; Fungal Proteins/metabolism; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; NADP/chemistry; NADP/metabolism; Oxidation-Reduction; Protein Structure, Secondary; Protein Structure, Tertiary; Quinone Reductases/chemistry; Quinone Reductases/genetics; Quinone Reductases/metabolism; Recombinant Proteins/chemistry; Recombinant Proteins/genetics; Recombinant Proteins/metabolism; Repressor Proteins/chemistry; Repressor Proteins/genetics; Repressor Proteins/metabolism; Sequence Alignment |
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