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 2
Overall structure of BoSDR. (a) Like other SDRs, the protomer of BoSDR has a central β-sheet flanked by α-helices. The NAD⁺ coenzyme is shown in ball-and-stick representation with purple C atoms. Other heteroatoms are shown using standard coloring. Here, β-sheets are shown in green, α-helices are shown in blue and loops are in yellow. (b) The overall structure of BoSDR is tetrameric. Chain A is colored red, chain B is orange, chain C is colored by secondary structure as in (a) and chain D is yellow. The NAD⁺ is shown in ball-and-stick representation with the coloring as in (a).

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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