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Advanced filters: Author: Jaeok Park Clear advanced filters

Human farnesyl pyrophosphate synthase is allosterically inhibited by its own product

Farnesyl pyrophosphate (FPP) is a key building block for the synthesis of many lipids. Here the authors determine the crystal structure of farnesyl pyrophosphate synthase (FPPS) with its bound product and use kinetic measurements to show that FPP is an allosteric effector of the enzyme.

Jaeok Park
Michal Zielinski
Albert M. Berghuis
ResearchOpen Access18 Jan 2017
Nature Communications

Volume: 8, P: 1-8
Structural and functional insights into esterase-mediated macrolide resistance

Erythromycin esterases (Eres) cleave the macrolactone ring of macrolides, a class of widely used antibiotics. Structures of EreC, in silico flexible docking studies and previous mutagenesis data lead to the proposal of a detailed catalytic mechanism for the Ere family of enzymes.

Michał Zieliński
Jaeok Park
Albert M. Berghuis
ResearchOpen Access19 Mar 2021
Nature Communications

Volume: 12, P: 1-9
The Structural Dynamics of Engineered β-Lactamases Vary Broadly on Three Timescales yet Sustain Native Function

Sophie M. C. Gobeil
Maximillian C. C. J. C. Ebert
Joelle N. Pelletier
ResearchOpen Access30 Apr 2019
Scientific Reports

Volume: 9, P: 1-12
Structural and phylogenetic analyses of resistance to next-generation aminoglycosides conferred by AAC(2′) enzymes

Angelia V. Bassenden
Linda Dumalo
Albert M. Berghuis
ResearchOpen Access02 Jun 2021
Scientific Reports

Volume: 11, P: 1-13