7A2D

Structure-function analyses of dual-BON domain protein DolP identifies phospholipid binding as a new mechanism for protein localisation to the cell division site

Summary for 7A2D

• Entry DOI: 10.2210/pdb7a2d/pdb
• NMR Information: BMRB: 34552
• Descriptor: Uncharacterized protein YraP (1 entity in total)
• Functional Keywords: outer membrane biogenesis, gram negative, lipoprotein, yrap, lipid biogenesis, protein binding
• Biological source: Escherichia coli (strain K12)
• Total number of polymer chains: 1
• Total formula weight: 19324.74

Authors

Bryant, J.A.,Morris, F.C.,Knowles, T.J.,Maderbocus, R.,Heinz, E.,Boelter, G.,Alodaini, D.,Colyer, A.,Wotherspoon, P.J.,Staunton, K.A.,Jeeves, M.,Browning, D.F.,Sevastsyanovich, Y.R.,Wells, T.J.,Rossiter, A.E.,Bavro, V.N.,Sridhar, P.,Ward, D.G.,Chong, Z.S.,Goodall, E.C.A.,Icke, C.,Teo, A.,Chng, S.S.,Roper, D.I.,Lithgow, T.,Cunningham, A.F.,Banzhaf, M.,Overduin, M.,Henderson, I.R. (deposition date: 2020-08-17, release date: 2020-12-30, Last modification date: 2024-05-15)

Primary citation

Bryant, J.A.,Morris, F.C.,Knowles, T.J.,Maderbocus, R.,Heinz, E.,Boelter, G.,Alodaini, D.,Colyer, A.,Wotherspoon, P.J.,Staunton, K.A.,Jeeves, M.,Browning, D.F.,Sevastsyanovich, Y.R.,Wells, T.J.,Rossiter, A.E.,Bavro, V.N.,Sridhar, P.,Ward, D.G.,Chong, Z.S.,Goodall, E.C.,Icke, C.,Teo, A.C.,Chng, S.S.,Roper, D.I.,Lithgow, T.,Cunningham, A.F.,Banzhaf, M.,Overduin, M.,Henderson, I.R.
Structure of dual BON-domain protein DolP identifies phospholipid binding as a new mechanism for protein localisation.
Elife, 9:-, 2020

PubMed Abstract: 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 amongst Gram-negative bacteria and that loss of DolP increases membrane fluidity. We present the NMR solution structure for 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 localisation of the protein to the cell division site, providing evidence of subcellular localisation 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.

PubMed: 33315009
DOI: 10.7554/eLife.62614

Experimental method

SOLUTION NMR