EC Number   |
|---|
    2.7.6.3 | - |
| 2.7.6.3 | a complex of the purified protein with a substrate analog is crystallized and its structure is solved by multiple anomalous dispersion using phase information obtained from a single crystal of selenomethionine-labeled protein |
| 2.7.6.3 | apo W89A and its ternary complex with Mg-alpha,beta-methyleneadenosine triphosphate and 6-hydroxymethyl-7,8-dihydropterin are crystallized at 19°C using the hanging-drop vapor-diffusion technique. The structure of the ternary complex is determined at 1.25 A resolution |
| 2.7.6.3 | apoenzyme and in complex with substrate 6-hydroxymethyl-7,8-dihydropteridine or 2-(7-amino-1-methyl-4,5-dioxo-1,4,5,6-tetrahydorpyrimido[4,5-c]pyridazin-3-yl)propanoic acid, sitting drop vapor diffusion method, using 90 mM Tris (pH 8.0), 190 mM sodium acetate, 24% (w/v) polyethylene glycol (PEG) 4000, and 17% (v/v) glycerol, at 18°C |
| 2.7.6.3 | complexed with inhibitor 2-amino-7,7-dimethyl-4-oxo-3,4,7,8-tetrahydropteridine-6-carboxylic acid (2-[2-[5-(6-amino-purin-9-yl)-3,4-dihydroxy-tetrahydro-furan-2-ylmethanesulfonyl]-ethylcarbamoyl]-ethyl)-amide, sitting drop vapor diffusion method, using 25% (w/v) PEG 3350 and 0.2 M NaCl in 0.1 M HEPES, pH 7.5 |
| 2.7.6.3 | crystal structure of HPPk-DHPS in complex with four substrates/analogs. Sulfadoxine's effect on HPPK-DHPS is due to 4-amino benzoic acid mimicry, and resistance mutations surrounding the 4-amino benzoic acid-binding site are present within loop 2 (S382/F/A/Cand A383G), loop 5 (Lys512), loop 6 (Ala553), and 7' helix in loop7 (Val585) |
| 2.7.6.3 | crystallization of a complex of the purified bifunctional polypeptide with a pterin monophosphate substrate analogue, structure solved by molecular replacement and refined to 2.3 A resolution. Three-dimensional structure in complex with the oxidized substrate analogue 6-hydroxy-methyl-pterin monophosphate reveals how the HPPK and DHPS functional domains associate at both the ternary and quaternary levels |
| 2.7.6.3 | hanging-drop method |
| 2.7.6.3 | hanging-drop vapor-diffusion method. At 0.89-A resolution, two distinct conformations are observed for each of the two residues in the crystal structure of the wild-type enzyme in complex with two 6-hydroxymethyl-7,8-dihydropterin variants, two Mg2+ ions, and an ATP analogue. 1. Complex of wild-type enzyme with 6-hydroxymethylpterin, 6-carboxypterin and alpha,beta-methyleneadenosine 5'-triphosphate, 2. complex of mutant enzyme R82A with 6-hydroxymethyl-7,8-dihydropterin and alpha,beta-methyleneadenosine 5'-triphosphate, 3. complex of mutant enzyme R92A with 6-hydroxymethyl-7,8-dihydropterin and alpha,beta-methyleneadenosine 5'-triphosphate, 4. matant apoenzyme of R82A, 5. mutant apoenzyme of R92A, 6. mutant enzyme R92A in complex with Mg2+ |
| 2.7.6.3 | in complex with 2-amino-6-[(2-{4-[5-(6-amino-purin-9-yl)-3,4-dihydroxy-tetrahydrofuran-2-ylmethylsulfanyl]-piperidin-1-yl}-ethylamino)-methyl]-3H-pteridin-4-one, 2-amino-6-[(2-{4-[5-(6-amino-purin-9-yl)-3,4-dihydroxy-tetrahydrofuran-2-ylmethylsulfanyl]-piperidin-1-yl}-ethylamino)-methyl]-7,7-dimethyl-7,8-dihydro-3H pteridin-4-one, or 2-amino-7,7-dimethyl-4-oxo-3,4,7,8-tetrahydro-pteridine-6-carboxylic acid (2-{4-[5-(6-amino-purin-9-yl)-3,4-dihydroxy-tetrahydro-furan-2-ylmethylsulfanyl]-piperidin-1-yl}-ethyl)-amide, sitting drop vapor diffusion method, using 20% or 25% (w/v) PEG 3350 as precipitant, at 19°C |
