Crystallization (Comment) | Organism |
---|---|
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 | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
soluble | - |
Thermus thermophilus | - |
- |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Thermus thermophilus | Q8L3C8 | - |
- |
Thermus thermophilus HB8 / ATCC 27634 / DSM 579 | Q8L3C8 | - |
- |
Synonyms | Comment | Organism |
---|---|---|
Qor | - |
Thermus thermophilus |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
80 | - |
thermal denaturation | Thermus thermophilus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
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 |