Structural highlights
Function
[EMTA_ECOLI] Murein-degrading enzyme. May play a role in recycling of muropeptides during cell elongation and/or cell division. Preferentially cleaves at a distance of more than two disaccharide units from the ends of the glycan chain. Prefers cross-linked murein in vivo.
Publication Abstract from PubMed
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.
High-Resolution Crystal Structure of MltE, an Outer Membrane-Anchored Endolytic Peptidoglycan Lytic Transglycosylase from Escherichia coli.,Artola-Recolons C, Carrasco-Lopez C, Llarrull LI, Kumarasiri M, Lastochkin E, Martinez de Ilarduya I, Meindl K, Uson I, Mobashery S, Hermoso JA Biochemistry. 2011 Apr 5;50(13):2384-2386. Epub 2011 Mar 8. PMID:21341761[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Artola-Recolons C, Carrasco-Lopez C, Llarrull LI, Kumarasiri M, Lastochkin E, Martinez de Ilarduya I, Meindl K, Uson I, Mobashery S, Hermoso JA. High-Resolution Crystal Structure of MltE, an Outer Membrane-Anchored Endolytic Peptidoglycan Lytic Transglycosylase from Escherichia coli. Biochemistry. 2011 Apr 5;50(13):2384-2386. Epub 2011 Mar 8. PMID:21341761 doi:10.1021/bi200085y
