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Structure of the catalytic domain of the colistin resistance enzyme MCR-1

Overview of attention for article published in BMC Biology, September 2016
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Title
Structure of the catalytic domain of the colistin resistance enzyme MCR-1
Published in
BMC Biology, September 2016
DOI 10.1186/s12915-016-0303-0
Pubmed ID
Authors

Vlatko Stojanoski, Banumathi Sankaran, B. V. Venkataram Prasad, Laurent Poirel, Patrice Nordmann, Timothy Palzkill

Abstract

Due to the paucity of novel antibiotics, colistin has become a last resort antibiotic for treating multidrug resistant bacteria. Colistin acts by binding the lipid A component of lipopolysaccharides and subsequently disrupting the bacterial membrane. The recently identified plasmid-encoded MCR-1 enzyme is the first transmissible colistin resistance determinant and is a cause for concern for the spread of this resistance trait. MCR-1 is a phosphoethanolamine transferase that catalyzes the addition of phosphoethanolamine to lipid A to decrease colistin affinity. The structure of the catalytic domain of MCR-1 at 1.32 Å reveals the active site is similar to that of related phosphoethanolamine transferases. The putative nucleophile for catalysis, threonine 285, is phosphorylated in cMCR-1 and a zinc is present at a conserved site in addition to three zincs more peripherally located in the active site. As noted for catalytic domains of other phosphoethanolamine transferases, binding sites for the lipid A and phosphatidylethanolamine substrates are not apparent in the cMCR-1 structure, suggesting that they are present in the membrane domain.

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The data shown below were compiled from readership statistics for 119 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Paraguay 1 <1%
Unknown 118 99%

Demographic breakdown

Readers by professional status Count As %
Student > Bachelor 23 19%
Student > Master 21 18%
Student > Ph. D. Student 16 13%
Researcher 15 13%
Student > Postgraduate 6 5%
Other 13 11%
Unknown 25 21%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 29 24%
Agricultural and Biological Sciences 17 14%
Immunology and Microbiology 12 10%
Chemistry 12 10%
Medicine and Dentistry 9 8%
Other 11 9%
Unknown 29 24%