6SUT

Crystal structure of phosphothreonine MCR-2

Summary for 6SUT

Entry DOI	10.2210/pdb6sut/pdb
Descriptor	Putative integral membrane protein, ZINC ION, GLYCEROL, ... (5 entities in total)
Functional Keywords	colistin, mcr, phosphoethanolamine, transferase, antimicrobial protein
Biological source	Escherichia coli
Total number of polymer chains	1
Total formula weight	36674.90
Authors	Hinchliffe, P.,Spencer, J. (deposition date: 2019-09-16, release date: 2020-06-03, Last modification date: 2024-11-20)
Primary citation	Lythell, E.,Suardiaz, 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. Resistance to the "last resort" antibiotic colistin: a single-zinc mechanism for phosphointermediate formation in MCR enzymes. Chem.Commun.(Camb.), 56:6874-6877, 2020 Cited by PubMed 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. PubMed: 32432618 DOI: 10.1039/d0cc02520h PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.2 Å)

Structure validation