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1.
Fig. 3

Fig. 3. From: The mechanism of discrimination between oxidized and reduced coenzyme in the aldehyde dehydrogenase domain of Aldh1l1.

Comparison of structures of NADP+ (left) and thio-NADP+(right).

Yaroslav Tsybovsky, et al. Chem Biol Interact. 2013 February 25;202(1-3):62-69.
2.
Fig, 1

Fig, 1. From: The mechanism of discrimination between oxidized and reduced coenzyme in the aldehyde dehydrogenase domain of Aldh1l1.

The covalent bond between Cys707 of Ct-FDH and C4N of the nicotinamide ring of NADP+. Two positions of the sulfur, one forming the covalent bond (1.6 Å distance to C4N) and another oriented away from the nicotinamide ring (4 Å distance to C4N) are shown (green).

Yaroslav Tsybovsky, et al. Chem Biol Interact. 2013 February 25;202(1-3):62-69.
3.
Fig. 2

Fig. 2. From: The mechanism of discrimination between oxidized and reduced coenzyme in the aldehyde dehydrogenase domain of Aldh1l1.

NADP+ and NADPH molecules in the structures with C707S Ct-FDH. A superposition of the active sites of the C707S enzyme (colored) with bound NADP+ (A) or NADPH (B) and wt Ct-FDH-NADP+ complex or C707A enzyme-NADPH complex (grey), respectively. The 2∣FO∣-∣FC∣ electron density map of the coenzyme contoured at 1 σ is shown in blue.

Yaroslav Tsybovsky, et al. Chem Biol Interact. 2013 February 25;202(1-3):62-69.
4.
Fig. 4

Fig. 4. From: The mechanism of discrimination between oxidized and reduced coenzyme in the aldehyde dehydrogenase domain of Aldh1l1.

Binding of thio-NADP+ to Ct-FDH. (A) The active site of wild-type Ct-FDH with bound thio-NADP+ (the 2∣FO∣-∣FC∣ electron density map of thio-NADP+ contoured at 1 σ is shown in blue). (B) Overlay of coenzymes bound to ALDHs: grey, NADP+ (extended conformation) bound to wt Ct-FDH; orange, NADPH (contracted conformation) bound to ALDH2 [9]; violet, thio-NADP+ (contracted conformation) bound to wt Ct-FDH. (C) Environment of Glu673 in the complex of Ct-FDH with NADP+ (PDB 2O2Q).

Yaroslav Tsybovsky, et al. Chem Biol Interact. 2013 February 25;202(1-3):62-69.
5.
Fig. 5

Fig. 5. From: The mechanism of discrimination between oxidized and reduced coenzyme in the aldehyde dehydrogenase domain of Aldh1l1.

Proposed changes in the active site of Ct-FDH with the oxidized or reduced coenzyme bound at different stages of catalysis. A and B, bound NADP+ without and with formation of the covalent bond between Cys707 and the nicotinamide ring, respectively. C and D, NADPH bound in the extended (modeled from the C707A enzyme structure, PDB 3RHR [23]) or contracted (modeled from wt Ct-FDH/thio-NADP+ complex) conformation, correspondingly.

Yaroslav Tsybovsky, et al. Chem Biol Interact. 2013 February 25;202(1-3):62-69.
6.
Fig. 6

Fig. 6. From: The mechanism of discrimination between oxidized and reduced coenzyme in the aldehyde dehydrogenase domain of Aldh1l1.

Model depicting interactions of the coenzyme with ordered (A) or distorted (B) helix G. The model proposes that more ordered helix G is formed upon the coenzyme binding and the movement of catalytic glutamate outside of the nicotinamide binding part of the catalytic pocket. The helix presumably becomes distorted upon the return of catalytic glutamate back into the pocket that allows the dissociation of the coenzyme from the protein. Panel B was modeled based on the structure of the apo E673Q enzyme (PDB 3RHM [23]) and the structure of wt Ct-FDH in complex with thio-NADP+

Yaroslav Tsybovsky, et al. Chem Biol Interact. 2013 February 25;202(1-3):62-69.

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