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Literature summary extracted from

  • Shimomura, Y.; Kakuta, Y.; Fukuyama, K.
    Crystal structures of the quinone oxidoreductase from Thermus thermophilus HB8 and its complex with NADPH: Implication for NADPH and substrate recognition (2003), J. Bacteriol., 185, 4211-4218.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.6.5.5 native enzyme and its complex with NADPH at 2.3 A and 2.8 A resolution. QOR forms a homodimer in the crystal by interaction of the betaF-strands in domain II, forming a large beta-sheet that crosses the dimer interface. NADPH is located between the two domains in the QOR-NADPH complex. The disordered segment involved in the coenzyme binding of apo-QOR becomes ordered upon NADPH binding. The segment covers an NADPH-binding cleft and may serve as a lid. The 2'-phosphate group of the adenine of NADPH is surrounded by polar and positively charged residues in QOR, suggesting that QOR binds NADPH more readily than NADH. The putative substrate-binding site of QOR, is largely blocked by nearby residues Thermus thermophilus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.6.5.5 soluble
-
 Thermus thermophilus
-
-

Organism

EC Number Organism UniProt Comment Textmining
1.6.5.5 Thermus thermophilus Q8L3C8
-
-
1.6.5.5 Thermus thermophilus HB8 / ATCC 27634 / DSM 579 Q8L3C8
-
-

Synonyms

EC Number Synonyms Comment Organism
1.6.5.5 Qor
-
 Thermus thermophilus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.6.5.5 80
-
 thermal denaturation Thermus thermophilus

Cofactor

EC Number Cofactor Comment Organism Structure
1.6.5.5 NADPH NADPH is located in the cleft between domains I and II. The adenine ring is sandwiched between the main chains of Ala220 and Glu221 and the side chain of Arg292. Ala220 and Glu221 are disordered in apo-QOR Thermus thermophilus