Crystal structure of dihydroorotate dehydrogenase from Helicobacter pylori with bound flavin mononucleotide

Agarwal, A.A.; Georgiades, J.D.; Dranow, D.M.; Lorimer, D.D.; Edwards, T.; Barrett, K.F.; Craig, J.K.; Van Voorhis, W.C.; Myler, P.J.; Smith, C.L.

doi:10.1107/S2053230X25000858

Figure 5
The N-terminal microdomain forms the membrane–protein interface and a ubiquinone channel. (a) Electrostatic surface plots of dihydroorotate dehydrogenase (DHODH) from H. pylori (PDB entry 6b8s chain A) and E. coli (PDB entry 1f76 chain A), viewing the N-terminal microdomain. Important residues are specified by arrows and labelled using one-letter codes. The colour blue represents high electropositivity and red represents high electronegativity in units of k_BT/e_c. (b) Hydrophobic amino acids (orange) line the centre of the N-terminal microdomain (blue), with charged residues (purple) at the solvent-accessible border; all residues are labelled using their one-letter codes. Background DHODH protein is coloured dark green. (c) Ubiquinone channel connecting the membrane to the flavin mononucleotide (FMN) binding site. View down the channel (cream colour) to FMN (yellow sticks). Background DHODH protein is coloured dark green. (d) The left and right panels show the protein interior, highlighting the residues that form the ubiquinone channel (cream colour). Hydrophobic amino acids (orange) and charged amino acids (purple) are labelled using one-letter codes. FMN (yellow sticks) is shown in the FMN binding pocket that is connected to the ubiquinone channel. Background DHODH protein is coloured dark green.

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

Volume 81| Part 3| March 2025| Pages 108-117

https://doi.org/10.1107/S2053230X25000858

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