Crystal structure of a short-chain dehydrogenase from Burkholderia cenocepacia J2315 in complex with NADP+ and benzoic acid

Belfon, K.K.J.; Beyer, O.; Abendroth, J.; Dranow, D.M.; Lorimer, D.D.; Abramov, A.; Latimore, Y.; Hamilton, C.; Dawkins, A.; Hinojosa, I.; Martinez, X.; Mirabel, S.; Duncan, M.; Womack, R.; Hicks, L.; Turlington, Z.R.; Edwards, T.E.; Torelli, A.T.; Hicks, K.A.; French, J.B.

doi:10.1107/S2053230X24011282

Acta Crystallographica Section F
Acta Crystallographica
Section F STRUCTURAL BIOLOGY COMMUNICATIONS

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Figure 2
Overall structure of BcSDR. The protomer of BcSDR has a central β-sheet flanked by α-helices on each side (a) with NADP⁺ (ball-and-stick representation) bound in the cofactor-binding site and benzoic acid (wire representation) bound in the active site. α-Helices are shown in blue, β-sheets are shown in green and loops are shown in yellow. NADP⁺ and benzoic acid are depicted with green C atoms, red O atoms, blue N atoms and orange P atoms. The active form of BcSDR is a dimer (b). Chain A, NADP⁺ and benzoic acid are colored as in (a). Chain B is colored red.

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

Volume 80| Part 12| December 2024| Pages 348-355

https://doi.org/10.1107/S2053230X24011282

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