Emily Lythell,‡ab Reynier Suardiaz,‡acde Philip Hinchliffe,‡b Chonnikan Hanpaibool,f Surawit Visitsatthawong,g A. Sofia F. Oliveira,ac Eric J. M. Lang,a Panida Surawatanawong,g Vannajan Sanghiran Lee,h Thanyada Rungrotmongkol,fi Natalie Fey,a James Spencerb and Adrian J. Mulhollanda
a Centre for Computational Chemistry, School of Chemistry, University of Bristol, Cantock’s Close, Bristol, BS8 1TS, UK. E-mail: Adrian.Mulholland@bristol.ac.uk
b School of Cellular and Molecular Medicine, University of Bristol, University Walk, Bristol, BS8 1TD, UK. E-mail: Jim.Spencer@bristol.ac.uk
c School of Biochemistry, University of Bristol, University Walk, Bristol, BS8 1TD, UK
d Centre for Enzyme Innovation, School of Biological Sciences, Institute of Biological and Biomedical Sciences, University of Portsmouth, Portsmouth PO1 2DT, UK
e Department of Physical Chemistry, Faculty of Chemistry, Complutense University of Madrid, 28040 Madrid, Spain
f Structural and Computational Biology Research Unit, Department of Biochemistry, Faculty of Science, Chulalongkorn University, Bangkok
10330, Thailand
g Department of Chemistry and Center of Excellence for Innovation in Chemistry, Faculty of Science, Mahidol University, Bangkok 10400,
Thailand
h Department of Chemistry, Faculty of Science, University of Malaya, Kuala Lumpur 50603, Malaysia
i Program in Bioinformatics and Computational Biology, Graduate School, Chulalongkorn University, Bangkok 10330, Thailand
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.
Reference: Lythell, E.; Suardíaz, R.; Hinchliffe, P.; Hanpaibool, C.; Visitsatthawong, S.; Oliveira, A. S. F.; Lang, E. J.
M.; Surawatanawong, P.; Lee, V. S.; Rungrotmongkol, T.; Fey, N.; Spencer, J.; Mulholland, A. J. Chem. Commun.
2020, 56, 6874-6877. https://doi.org/10.1039/D0CC02520H