Crystal structures of FolM alternative dihydrofolate reductase 1 from Brucella suis and Brucella canis

Porter, I.; Neal, T.; Walker, Z.; Hayes, D.; Fowler, K.; Billups, N.; Rhoades, A.; Smith, C.; Smith, K.; Staker, B.L.; Dranow, D.M.; Mayclin, S.J.; Subramanian, S.; Edwards, T.E.; Myler, P.J.; Asojo, O.A.

doi:10.1107/S2053230X21013078

Acta Crystallographica Section F
Acta Crystallographica
Section F STRUCTURAL BIOLOGY COMMUNICATIONS

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Figure 3
Two views comparing BsFolM and BcFolM monomers with similar structures. The BsFolM and BcFolM monomers (gray) have the prototypical double-Rossmann fold of NADPH-dependent short-chain dehydrogenase/reductases observed in the molecular-replacement search model (tan) and protozoan pteridine reductase (green). The superposed protozoan structures are Trypanosoma brucei pteridine reductase with cyromazine (PDB entry 2x9n; cyan green), T. brucei pteridine reductase ternary complex with cofactor and inhibitor (PDB entry 4cm8; dark green) and T. cruzi pteridine reductase (PDB entry 1mxf; light green). The cofactor NADPH is shown in blue sticks, while the inhibitor from PDB entry 1mxf is shown as magenta sticks in the substrate-binding cavity. As in Fig. 2

, SBC stands for substrate-binding cavity.

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

Volume 78| Part 1| January 2022| Pages 31-38

https://doi.org/10.1107/S2053230X21013078

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