2Y8P

Crystal Structure of an Outer Membrane-Anchored Endolytic Peptidoglycan Lytic Transglycosylase (MltE) from Escherichia coli

Summary for 2Y8P

• Entry DOI: 10.2210/pdb2y8p/pdb
• Descriptor: ENDO-TYPE MEMBRANE-BOUND LYTIC MUREIN TRANSGLYCOSYLASE A (2 entities in total)
• Functional Keywords: lyase, cell wall biogenesis/degradation
• Biological source: ESCHERICHIA COLI
• Cellular location: Cell outer membrane; Lipid-anchor (Probable): P0C960
• Total number of polymer chains: 2
• Total formula weight: 42828.62

Authors

Artola-Recolons, C.,Carrasco-Lopez, C.,Llarrull, L.I.,Kumarasiri, M.,Lastochkin, E.,Martinez-Ilarduya, I.,Meindl, K.,Uson, I.,Mobashery, S.,Hermoso, J.A. (deposition date: 2011-02-08, release date: 2011-04-13, Last modification date: 2024-05-08)

Primary citation

Artola-Recolons, C.,Carrasco-Lopez, C.,Llarrull, L.I.,Kumarasiri, M.,Lastochkin, E.,Martinez De Ilarduya, I.,Meindl, K.,Uson, I.,Mobashery, S.,Hermoso, J.A.
High-Resolution Crystal Structure of Mlte, an Outer Membrane-Anchored Endolytic Peptidoglycan Lytic Transglycosylase from Escherichia Coli.
Biochemistry, 50:2384-, 2011

PubMed Abstract: 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.

PubMed: 21341761
DOI: 10.1021/BI200085Y

Experimental method

X-RAY DIFFRACTION (1.995 Å)