2KM7

Solution Structure of BamE, a component of the outer membrane protein assembly machinery in Escherichia coli

2KM7 の概要

• エントリーDOI: 10.2210/pdb2km7/pdb
• 分子名称: Small protein A (1 entity in total)
• 機能のキーワード: bame, smpa, bam complex, omp85, yaet, cell membrane, cell outer membrane, lipoprotein, membrane, palmitate, membrane protein
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cell outer membrane; Lipid-anchor: P0A937
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11446.64

構造登録者

Knowles, T.J.,Sridhar, P.,Rajesh, S.,Manoli, E.,Henderson, I.R.,Overduin, M. (登録日: 2009-07-24, 公開日: 2011-02-02, 最終更新日: 2024-05-22)

主引用文献

Knowles, T.J.,Browning, D.F.,Jeeves, M.,Maderbocus, R.,Rajesh, S.,Sridhar, P.,Manoli, E.,Emery, D.,Sommer, U.,Spencer, A.,Leyton, D.L.,Squire, D.,Chaudhuri, R.R.,Viant, M.R.,Cunningham, A.F.,Henderson, I.R.,Overduin, M.
Structure and function of BamE within the outer membrane and the beta-barrel assembly machine.
Embo Rep., 12:123-128, 2011

PubMed Abstract: Insertion of folded proteins into the outer membrane of Gram-negative bacteria is mediated by the essential β-barrel assembly machine (Bam). Here, we report the native structure and mechanism of a core component of this complex, BamE, and show that it is exclusively monomeric in its native environment of the periplasm, but is able to adopt a distinct dimeric conformation in the cytoplasm. BamE is shown to bind specifically to phosphatidylglycerol, and comprehensive mutagenesis and interaction studies have mapped key determinants for complex binding, outer membrane integrity and cell viability, as well as revealing the role of BamE within the Bam complex.

PubMed: 21212804
DOI: 10.1038/embor.2010.202

実験手法

SOLUTION NMR