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 6
Structural alignment of BoSDR with its closest homologues. The structures are shown in cartoon representation colored by structure. Any bound ions or small molecules are shown in ball-and-stick representation with the same coloring as the protein structure. BoSDR is shown in pink, its closest structural homologue FabG (PDB entry 4nbv) is shown in orange and 2,3-butanediol dehydrogenase (PDB entry 6vsp) is shown in yellow, including a bound sodium cation. The ketoreductase from Sphingobacterium siyangense SY1 (PDB entry 8y83) is shown in green and the ketone reductase ChKRED20 from Chryseobacterium sp. CA49 is shown in blue (PDB entry 6ixm). For clarity, only a single protomer of each protein is depicted. The cavity leading to the active site is highlighted with a box.

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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