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

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 cataly

SUBMITTER: Stojanoski V 

PROVIDER: S-EPMC5031297 | biostudies-literature | 2016 Sep

REPOSITORIES: biostudies-literature