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Resistance to the “last resort” antibiotic colistin: a single-zinc mechanism for phosphointermediate formation in MCR enzymes

DOI: 10.1039/D0CC02520H DOI Help

Authors: Emily Lythell (University of Bristol) , Reynier Suardíaz (University of Bristol; University of Portsmouth; University of Madrid) , Philip Hinchliffe (University of Bristol) , Chonnikan Hanpaibool (Chulalongkorn University) , Surawit Visitsatthawong (Mahidol University) , A. Sofia F. Oliveira (University of Bristol) , Eric J. M. Lang (University of Bristol) , Panida Surawatanawong (Mahidol University) , Vannajan Sanghiran Lee (University of Malaya) , Thanyada Rungrotmongkol (Chulalongkorn University) , Natalie Fey (University of Bristol) , James Spencer (University of Bristol) , Adrian J. Mulholland (University of Bristol)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Chemical Communications , VOL 35

State: Published (Approved)
Published: May 2020
Diamond Proposal Number(s): 12342

Abstract: MCR (mobile colistin resistance) enzymes catalyse phosphoethanolamine (PEA) addition to bacterial lipid A, threatening the “last-resort” antibiotic colistin. Molecular dynamics and density functional theory simulations indicate that monozinc MCR supports PEA transfer to the Thr285 acceptor, positioning MCR as a mono- rather than multinuclear member of the alkaline phosphatase superfamily.

Diamond Keywords: Enzymes; Bacteria

Subject Areas: Biology and Bio-materials, Chemistry, Medicine

Instruments: I24-Microfocus Macromolecular Crystallography

Added On: 03/06/2020 09:14


Discipline Tags:

Catalysis Organic Chemistry Life Sciences & Biotech Health & Wellbeing Antibiotic Resistance Drug Discovery Pathogens Structural biology Chemistry

Technical Tags:

Diffraction Macromolecular Crystallography (MX)