Unknown

Dataset Information

0

Crystal structure of type II NADH:quinone oxidoreductase from Caldalkalibacillus thermarum with an improved resolution of 2.15?A.


ABSTRACT: Type II NADH:quinone oxidoreductase (NDH-2) is a respiratory enzyme found in the electron-transport chain of many species, with the exception of mammals. It is a 40-70?kDa single-subunit monotopic membrane protein that catalyses the oxidation of NADH and the reduction of quinone molecules via the cofactor FAD. NDH-2 is a promising new target for drug development given its essential role in many bacterial species and intracellular parasites. Only two bacterial NDH-2 structures have been reported and these structures are at moderate resolution (2.3-2.5?Å). In this communication, a new crystallization platform is reported that produced high-quality NDH-2 crystals that diffracted to high resolution (2.15?Å). The high-resolution NDH-2 structure was used for in silico quinone substrate-docking studies to investigate the binding poses of menadione and ubiquinone molecules. These studies revealed that a very limited number of molecular interactions occur at the quinone-binding site of NDH-2. Given that the conformation of the active site is well defined, this high-resolution structure is potentially suitable for in silico inhibitor-compound screening and ligand-docking applications.

SUBMITTER: Nakatani Y 

PROVIDER: S-EPMC5633920 | biostudies-literature | 2017 Oct

REPOSITORIES: biostudies-literature

altmetric image

Publications

Crystal structure of type II NADH:quinone oxidoreductase from Caldalkalibacillus thermarum with an improved resolution of 2.15 Å.

Nakatani Yoshio Y   Jiao Wanting W   Aragão David D   Shimaki Yosuke Y   Petri Jessica J   Parker Emily J EJ   Cook Gregory M GM  

Acta crystallographica. Section F, Structural biology communications 20170923 Pt 10


Type II NADH:quinone oxidoreductase (NDH-2) is a respiratory enzyme found in the electron-transport chain of many species, with the exception of mammals. It is a 40-70 kDa single-subunit monotopic membrane protein that catalyses the oxidation of NADH and the reduction of quinone molecules via the cofactor FAD. NDH-2 is a promising new target for drug development given its essential role in many bacterial species and intracellular parasites. Only two bacterial NDH-2 structures have been reported  ...[more]

Similar Datasets

| S-EPMC2168623 | biostudies-literature
| S-EPMC5857484 | biostudies-literature
| S-EPMC4274662 | biostudies-literature
| S-EPMC5299459 | biostudies-literature
| S-EPMC3297363 | biostudies-literature
| S-EPMC3351724 | biostudies-literature
| S-EPMC2998382 | biostudies-literature
| S-EPMC6295900 | biostudies-literature
| S-EPMC6560451 | biostudies-literature
| S-EPMC14730 | biostudies-literature