Crystal structure of a short-chain dehydrogenase from Brucella ovis with apo and coenzyme NAD+-bound protomer chains

Zupko, S.P.; Konstanty, A.T.; Mayclin, S.J.; Choi, R.; Serbzhinskiy, D.; Robles, E.; Moses, V.; Barrett, L.K.; Van Voorhis, W.C.; Edwards, T.E.; Myler, P.J.; Torelli, A.T.; French, J.B.; Hicks, K.A.

doi:10.1107/S2053230X25009227

Acta Crystallographica Section F
Acta Crystallographica
Section F STRUCTURAL BIOLOGY COMMUNICATIONS

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Figure 5
Putative active site of BoSDR. (a) The putative active site of BoSDR is depicted with the secondary structure colored as in Fig. 2

(a). For clarity, only the active site of chain C is shown. C atoms are shown in cyan. Other heteroatoms are shown using standard coloring. For clarity, water molecules are not shown. A hydrogen bond (3.0 Å) between Lys167 and the 3′-OH of NAD⁺ is depicted. (b) A potential mechanism for the BoSDR-catalyzed reaction is shown based on the active-site architecture and the mechanism of other classical SDRs (Filling et al., 2002

). For clarity, only the oxidation of an alcohol is shown. Here, R refers to the rest of the substrate molecule and R₁ to the rest of the NAD⁺ coenzyme molecule.

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

Volume 81| Part 12| December 2025| Pages 487-494

https://doi.org/10.1107/S2053230X25009227

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