5K4P

Catalytic Domain of MCR-1 phosphoethanolamine transferase

Summary for 5K4P

Entry DOI	10.2210/pdb5k4p/pdb
Descriptor	Probable phosphatidylethanolamine transferase Mcr-1, ZINC ION, sorbitol, ... (4 entities in total)
Functional Keywords	phosphoethanolamine transferase, alpha/beta/alpha fold, alkaline phosphatase superfamily, transferase
Biological source	Escherichia coli BL21(DE3)
Total number of polymer chains	1
Total formula weight	39345.18
Authors	Stojanoski, V.,Palzkill, T.,Prasad, B.V.V.,Sankaran, B. (deposition date: 2016-05-21, release date: 2016-08-31, Last modification date: 2024-10-09)
Primary citation	Stojanoski, V.,Sankaran, B.,Prasad, B.V.,Poirel, L.,Nordmann, P.,Palzkill, T. Structure of the catalytic domain of the colistin resistance enzyme MCR-1. Bmc Biol., 14:81-81, 2016 Cited by PubMed 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. PubMed: 27655155 DOI: 10.1186/s12915-016-0303-0 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.318 Å)

Structure validation