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Figure 5
The NAD-binding site. (a) The `hydrolysis' [NAD–SaBADHBME(+/−); C atoms in yellow/gray] and `hydride-transfer' [NAD–G234S-SaBADHBME(−); 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 SaBADHBME(+)PEG (C atoms in black), apo SaBADHBME(+) (C atoms in green), apo SaBADHBME(−) (C atoms in pink), NAD–SaBADHBME(+) (C atoms in yellow), NAD–SaBADHBME(−) (C atoms in light gray), NAD–G234S-SaBADHBME(−) (C atoms in magenta), apo G234S-SaBADHBME(−) (C atoms in cyan) and apo G234S-SaBADHBME(+) (C atoms in orange). Cys289 and NAD+ in NAD–G234S-SaBADHBME(−) and NAD+ in NAD–SaBADHBME(+) 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)].

Journal logoSTRUCTURAL
BIOLOGY
ISSN: 2059-7983
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