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EC Number	Crystallization (Commentary)
1.1.1.367	hanging-drop vapour-diffusion method, optimization of the crystallization conditions by differential scanning calorimetry affords a crystal of selenomethionine-substituted enzyme that diffracts to a resolution of 2.80 A. The crystals belong to space group P3(2)21, with unit-cell parameters a = b = 119.6, c = 129.5 A
1.1.1.367	in an open form of the apoenzyme. Enzyme CapF is a homodimer displaying a characteristic dumb-bell-shaped architecture composed of two domains. The N-terminal domain (residues 1-252) adopts a Rossmann fold belonging to the short-chain dehydrogenase/reductase family of proteins. The C-terminal domain (residues 252-369) displays a standard cupin fold with a Zn2+ ion bound deep in the binding pocket of the beta-barrel. The cupin domain is necessary for the C3-epimerization of UDP-4-hexulose. The N-terminal domain catalyses the NADPH-dependent reduction of the intermediate species generated by the cupin domain. A thermodynamic switch governs the attachment and release of the coenzyme NADPH during each catalytic cycle. suggesting that the binding of coenzyme to CapF facilitates a disorder-to-order transition in the catalytic loop of the reductase (N-terminal) domain

EC Number

Crystallization (Commentary)

1.1.1.367

hanging-drop vapour-diffusion method, optimization of the crystallization conditions by differential scanning calorimetry affords a crystal of selenomethionine-substituted enzyme that diffracts to a resolution of 2.80 A. The crystals belong to space group P3(2)21, with unit-cell parameters a = b = 119.6, c = 129.5 A

1.1.1.367

in an open form of the apoenzyme. Enzyme CapF is a homodimer displaying a characteristic dumb-bell-shaped architecture composed of two domains. The N-terminal domain (residues 1-252) adopts a Rossmann fold belonging to the short-chain dehydrogenase/reductase family of proteins. The C-terminal domain (residues 252-369) displays a standard cupin fold with a Zn2+ ion bound deep in the binding pocket of the beta-barrel. The cupin domain is necessary for the C3-epimerization of UDP-4-hexulose. The N-terminal domain catalyses the NADPH-dependent reduction of the intermediate species generated by the cupin domain. A thermodynamic switch governs the attachment and release of the coenzyme NADPH during each catalytic cycle. suggesting that the binding of coenzyme to CapF facilitates a disorder-to-order transition in the catalytic loop of the reductase (N-terminal) domain

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Release 2023.1 (January 2023)