EC Number   |
|---|
    1.1.1.28 | - |
| 1.1.1.28 | 1.9 A resolution |
| 1.1.1.28 | comparison of the apo and ternary complex structures of Fusobacterium nucleatum FnLDH and Escherichia coli EcLDH and Pseudomonas aeruginosa PaLDH. FnLDH and EcLDH exhibit positive cooperativity in substrate binding, and PaLDH shows negatively cooperative substrate binding. The three enzymes consistently form homotetrameric structures with three symmetric axes, the P-, Q-, and R-axes, which allows apo-FnLDH and EcLDH to form wide intersubunit contact surfaces between the opened catalytic domains of the two Q-axis-related subunits in coordination with their asymmetric and distorted quaternary structures. apo-PaLDH possesses a highly symmetrical quaternary structure and partially closed catalytic domains that are favorable for initial substrate binding and forms virtually no intersubunit contact surface between the catalytic domains |
| 1.1.1.28 | crystals belong to the orthorhombic space group, diffract beyond 3.0 A resolution |
| 1.1.1.28 | hanging drop vapour diffusion method |
| 1.1.1.28 | hexagonal and tetragonal crystal forms, tetragonal form diffracted to 3.0 A resolution |
| 1.1.1.28 | homology modeling of structure |
| 1.1.1.28 | molecular modeling and docking of substrates. D-LDH1 binds pyruvate using Tyr101, Arg235, and His296 by hydrogen bonds in the NADH-pyruvate-LDH1 complex |
| 1.1.1.28 | purified recombinant enzyme in fully closed formation with lactate or pyruvate bound to the active site of each subunit of the functional dimer, 0.001 ml of protein solution containing 20.3 mg/ml protein in 20 mM Tris-HCl buffer pH 8.0 containing 150 mM NaCl, is mixed with 0.001 ml of reservoir solution containing 0.1 M MES buffer, pH 6.0, and 25% w/v PEG 200, 10 days, method optimization, X-ray diffraction structure determination and analysis at 2.12 A resolution, molecular replacement and structure modelling |
| 1.1.1.28 | purified recombinant enzyme, hanging drop vapour diffusion method, mixing of 0.002 ml of 15 mg/ml protein in 10 mM potassium phosphate, pH 7.0, with 0.002 ml of reservoir solution containing 14.4% PEG 8000, 80 mM cacodylate pH 6.5, 160 mM calcium acetate and 20% glycerol, and equilibration against 0.1 ml of reservoir solution, 25°C, 2 weeks, X-ray diffraction structure determination and analysis at 2.0 A resolution |
