High-resolution crystal structure of MltE, an outer membrane-anchored endolytic peptidoglycan lytic transglycosylase from Escherichia coli

Biochemistry. 2011 Apr 5;50(13):2384-6. doi: 10.1021/bi200085y. Epub 2011 Mar 8.


The crystal structure of the first endolytic peptidoglycan lytic transglycosylase MltE from Escherichia coli is reported here. The degradative activity of this enzyme initiates the process of cell wall recycling, which is an integral event in the existence of bacteria. The structure sheds light on how MltE recognizes its substrate, the cell wall peptidoglycan. It also explains the ability of this endolytic enzyme to cleave in the middle of the peptidoglycan chains. Furthermore, the structure reveals how the enzyme is sequestered on the inner leaflet of the outer membrane.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Outer Membrane Proteins / chemistry*
  • Biocatalysis
  • Catalytic Domain
  • Crystallography, X-Ray
  • Escherichia coli / enzymology*
  • Escherichia coli Proteins / chemistry*
  • Models, Molecular
  • Peptidoglycan Glycosyltransferase / chemistry*
  • Protein Conformation
  • Substrate Specificity


  • Bacterial Outer Membrane Proteins
  • Escherichia coli Proteins
  • Peptidoglycan Glycosyltransferase

Associated data

  • PDB/2Y8P