Structural and functional analysis of betaine aldehyde dehydrogenase from Staphylococcus aureus

Halavaty, A.S.; Rich, R.L.; Chen, C.; Joo, J.C.; Minasov, G.; Dubrovska, I.; Winsor, J.R.; Myszka, D.G.; Duban, M.; Shuvalova, L.; Yakunin, A.F.; Anderson, W.F.

doi:10.1107/S1399004715004228

Figure 5
The NAD-binding site. (a) The `hydrolysis' [NAD–SaBADH^BME(+/−); C atoms in yellow/gray] and `hydride-transfer' [NAD–G234S-SaBADH^BME(−); C atoms in magenta] positions of NAD⁺. (b) The 3.0σ OMIT map (green mesh) of NAD⁺ in the NAD–(G234S-)SaBADH structures [chains A are displayed and colored as in (a)]. (c) The catalytic and nicotinamide ring-binding sites in the SaBADH structures: apo SaBADH^BME(+)PEG (C atoms in black), apo SaBADH^BME(+) (C atoms in green), apo SaBADH^BME(−) (C atoms in pink), NAD–SaBADH^BME(+) (C atoms in yellow), NAD–SaBADH^BME(−) (C atoms in light gray), NAD–G234S-SaBADH^BME(−) (C atoms in magenta), apo G234S-SaBADH^BME(−) (C atoms in cyan) and apo G234S-SaBADH^BME(+) (C atoms in orange). Cys289 and NAD⁺ in NAD–G234S-SaBADH^BME(−) and NAD⁺ in NAD–SaBADH^BME(+) are only shown for clarity. `Intermediate' and `inside' refer to the corresponding positions of the catalytic base Glu255. The bound PEG molecule at the NAD-binding site is not shown for clarity. The inset shows alternative conformations of the Leu256-Gly257 peptide bond and its possible role in supporting the `inside' conformation of Glu255 and the `hydride-transfer' position of NAD⁺; selected structures are shown and atoms are colored as in the main panel. (d) Attacking (A) and resting (R) conformations of Cys289 within all SaBADH structures [chains A are displayed; C atoms are colored as in (c)].

STRUCTURAL
BIOLOGY

ISSN: 2059-7983

Volume 71| Part 5| May 2015| Pages 1159-1175

https://doi.org/10.1107/S1399004715004228

Open

access

Search IUCr Journals		doi		Advanced search
Author		volume	page