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• W2037846585 endingPage "19253" @default.
• W2037846585 startingPage "19245" @default.
• W2037846585 abstract "In bacteria, the synthesis of the protective peptidoglycan sacculus is a dynamic process that is tightly regulated at multiple levels. Recently, the lipoprotein co-factor LpoB has been found essential for the in vivo function of the major peptidoglycan synthase PBP1b in Enterobacteriaceae. Here, we reveal the crystal structures of Salmonella enterica and Escherichia coli LpoB. The LpoB protein can be modeled as a ball and tether, consisting of a disordered N-terminal region followed by a compact globular C-terminal domain. Taken together, our structural data allow us to propose new insights into LpoB-mediated regulation of peptidoglycan synthesis." @default.
• W2037846585 created "2016-06-24" @default.
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• W2037846585 date "2014-07-01" @default.
• W2037846585 modified "2023-10-11" @default.
• W2037846585 title "Structural Insights into the Lipoprotein Outer Membrane Regulator of Penicillin-binding Protein 1B" @default.
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• W2037846585 doi "https://doi.org/10.1074/jbc.m114.565879" @default.
• W2037846585 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4081958" @default.
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• W2037846585 hasPublicationYear "2014" @default.
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