EC Number |
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1.1.1.25 | - |
1.1.1.25 | analysis of three-dimensional crystal structure of enzyme DHQD-SDH with shikimate bound in the SDH active site, PDB ID 2GPT. Crystallization of T381G mutant bound with quinate |
1.1.1.25 | apo-enzyme and in complex with both shikimate and NADP+, which assumes the closed conformation |
1.1.1.25 | at 4°C, using the hanging-drop vapor-diffusion method. SDH both in its ligand-free form and in complex with shikimate. Overall structure of apo-SDH is basically identical to that of the shikimate-SDH complex, both structures contain one molecule per asymmetric unit. Overall folding of SDH comprises the N-terminal alpha/beta domain for substrate binding and the C-terminal Rossmann fold for NADP binding. The active site is within a large groove between the two domains. Residue Tyr211 does not interact with shikimate in the binary SDH-shikimate complex structure. The main function of Tyr211 may be to stabilize the catalytic intermediate during catalysis. The NADP-binding domain of SDH is less conserved. The long helix specifically recognizing the adenine ribose phosphate is substituted with a short 310 helix in the NADP-binding domain. The interdomain angle of SDH is the widest among all known SDH structures, indicating an inactive open state of the SDH structure. Thus, a closing process may occur upon NADP+ binding to bring the cofactor close to the substrate for catalysis |
1.1.1.25 | catalytic domain with open twisted alpha/beta motif plus NADPH binding domain with typical Rossman fold |
1.1.1.25 | crystal structure analysis, PDB ID 2O7S |
1.1.1.25 | crystal structure analysis, PDB IDs 2GPT, 2O7Q, and 2O7S, for the binary and ternary complexes of enzyme and substrates |
1.1.1.25 | crystal structure determination of apoenzyme, PDB ID 3DON, and shikimate-bound binary enzyme complex, PDB ID 3DOO |
1.1.1.25 | crystal structure determination of the apoenzyme, PDB ID 4OMU |
1.1.1.25 | crystallized at 23°C using ammonium sulfate as a precipitant. Crystals grown in the presence of NADP+ diffract to 2.8 A resolution and belong to the trigonal space group P3(2)21 (or P3(2)21), with unit-cell parameters a = 111.3, b = 111.3, c = 76.2 A |