Structures of Pseudomonas aeruginosa β-ketoacyl-(acyl-carrier-protein) synthase II (FabF) and a C164Q mutant provide templates for antibacterial drug discovery and identify a buried potassium ion and a ligand-binding site that is an artefact of the crystal form

Baum, B.; Lecker, L.S.M.; Zoltner, M.; Jaenicke, E.; Schnell, R.; Hunter, W.N.; Brenk, R.

doi:10.1107/S2053230X15010614

Acta Crystallographica Section F
Acta Crystallographica
Section F STRUCTURAL BIOLOGY COMMUNICATIONS

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Figure 3
The active site. (a) A view into the narrow active-site cleft of the wild-type enzyme. The van der Waals radii are depicted as a grey semi-transparent surface. Residues are shown as sticks coloured by atomic position (purple, C; red, O; blue, N; yellow, S). Red spheres are waters. Three key catalytic residues are labelled. (b) Superposition of the wild-type and C164Q mutant active sites. The same colour scheme for atoms is used as in (a) except that the C atoms of the mutant are in orange. As a result of the C164Q mutation, Phe400 rotates out of the binding pocket.

STRUCTURAL BIOLOGY
COMMUNICATIONS

ISSN: 2053-230X

Volume 71| Part 8| August 2015| Pages 1020-1026

https://doi.org/10.1107/S2053230X15010614

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