| Literature DB >> 21341761 |
Cecilia Artola-Recolons1, César Carrasco-López, Leticia I Llarrull, Malika Kumarasiri, Elena Lastochkin, Iñaki Martínez de Ilarduya, Kathrin Meindl, Isabel Usón, Shahriar Mobashery, Juan A Hermoso.
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.Entities:
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Year: 2011 PMID: 21341761 PMCID: PMC3068208 DOI: 10.1021/bi200085y
Source DB: PubMed Journal: Biochemistry ISSN: 0006-2960 Impact factor: 3.162