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Publication Abstract from PubMed

The Gram-negative outer membrane envelops the bacterium and functions as a permeability barrier against antibiotics, detergents and environmental stresses. Some virulence factors serve to maintain the integrity of the outer membrane, including DolP (formerly YraP) a protein of unresolved structure and function. Here we reveal DolP is a lipoprotein functionally conserved among Gram-negative bacteria and that loss of DolP increases membrane fluidity. We present the NMR solution structure for Escherichia coli DolP, which is composed of two BON domains that form an interconnected opposing pair. The C-terminal BON domain binds anionic phospholipids through an extensive membrane:protein interface. This interaction is essential for DolP function and is required for sub-cellular localization of the protein to the cell division site, providing evidence of subcellular localization of these phospholipids within the outer membrane. The structure of DolP provides a new target for developing therapies that disrupt the integrity of the bacterial cell envelope.

Structure of dual-BON domain protein DolP identifies phospholipid binding as a new mechanism for protein localization.,Bryant JA, Morris FC, Knowles TJ, Maderbocus R, Heinz E, Boelter G, Alodaini D, Colyer A, Wotherspoon PJ, Staunton KA, Jeeves M, Browning DF, Sevastsyanovich YR, Wells TJ, Rossiter AE, Bavro VN, Sridhar P, Ward DG, Chong ZS, Goodall ECA, Icke C, Teo A, Chng SS, Roper DI, Lithgow T, Cunningham AF, Banzhaf M, Overduin M, Henderson IR Elife. 2020 Dec 14;9. pii: 62614. doi: 10.7554/eLife.62614. PMID:33315009^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.