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

7A2D の概要

• エントリーDOI: 10.2210/pdb7a2d/pdb
• NMR情報: BMRB: 34552
• 分子名称: Uncharacterized protein YraP (1 entity in total)
• 機能のキーワード: outer membrane biogenesis, gram negative, lipoprotein, yrap, lipid biogenesis, protein binding
• 由来する生物種: Escherichia coli (strain K12)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 19324.74

構造登録者

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. (登録日: 2020-08-17, 公開日: 2020-12-30, 最終更新日: 2024-05-15)

主引用文献

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

実験手法

SOLUTION NMR