2y8p | pdb_00002y8p

CRYSTAL STRUCTURE OF AN OUTER MEMBRANE-ANCHORED ENDOLYTIC PEPTIDOGLYCAN LYTIC TRANSGLYCOSYLASE (MLTE) FROM ESCHERICHIA COLI

spinqualitylabelsall models 2y8p, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2y8p is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, RCSB, PDBsum 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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