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Resistance to the “last resort” antibiotic colistin: a single-zinc mechanism for phosphointermediate formation in MCR enzymes
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.
Subject Areas:
Biology and Bio-materials,
Chemistry,
Medicine
Instruments:
I24-Microfocus Macromolecular Crystallography
Documents:
d0cc02520h.pdf