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

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Version: Final published version
Serval ID
serval:BIB_17386B94F005
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
Structure of the catalytic domain of the colistin resistance enzyme MCR-1.
Journal
Bmc Biology
Author(s)
Stojanoski V., Sankaran B., Prasad B.V., Poirel L., Nordmann P., Palzkill T.
ISSN
1741-7007 (Electronic)
ISSN-L
1741-7007
Publication state
Published
Issued date
2016
Peer-reviewed
Oui
Volume
14
Number
1
Pages
81
Language
english
Notes
Publication types: ARTICLE
Publication Status: epublish
Abstract
BACKGROUND: 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.
RESULTS: 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.
CONCLUSIONS: 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.
Pubmed
Web of science
Open Access
Yes
Create date
29/09/2016 18:47
Last modification date
20/08/2019 12:47
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