2ZCU
Crystal structure of a new type of NADPH-dependent quinone oxidoreductase (QOR2) from escherichia coli
Summary for 2ZCU
| Entry DOI | 10.2210/pdb2zcu/pdb |
| Related | 2ZCV |
| Descriptor | Uncharacterized oxidoreductase ytfG, COPPER (II) ION (3 entities in total) |
| Functional Keywords | alpha-beta sandwich, oxidoreductase |
| Biological source | ESCHERICHIA COLI |
| Total number of polymer chains | 1 |
| Total formula weight | 29825.95 |
| Authors | |
| Primary citation | Kim, I.K.,Yim, H.S.,Kim, M.K.,Kim, D.W.,Kim, Y.M.,Cha, S.S.,Kang, S.O. Crystal structure of a new type of NADPH-dependent quinone oxidoreductase (QOR2) from Escherichia coli J.Mol.Biol., 379:372-384, 2008 Cited by PubMed 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. PubMed: 18455185DOI: 10.1016/j.jmb.2008.04.003 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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