Steric hindrance controls pyridine nucleotide specificity of a flavin-dependent NADH:quinone oxidoreductase.

ABSTRACT: The crystal structure of the NADH:quinone oxidoreductase PA1024 has been solved in complex with NAD⁺ to 2.2 Å resolution. The nicotinamide C4 is 3.6 Å from the FMN N5 atom, with a suitable orientation for facile hydride transfer. NAD⁺ binds in a folded conformation at the interface of the TIM-barrel domain and the extended domain of the enzyme. Comparison of the enzyme-NAD⁺ structure with that of the ligand-free enzyme revealed a different conformation of a short loop (75-86) that is part of the NAD⁺ -binding pocket. P78, P82, and P84 provide internal rigidity to the loop, whereas Q80 serves as an active site latch that secures the NAD⁺ within the binding pocket. An interrupted helix consisting of two α-helices connected by a small thr

SUBMITTER: Ball J 

PROVIDER: S-EPMC6295900 | biostudies-literature | 2019 Jan

REPOSITORIES: biostudies-literature