5WAM

Structure of BamE from Neisseria gonorrhoeae

5WAM の概要

• エントリーDOI: 10.2210/pdb5wam/pdb
• 関連するPDBエントリー: 5WAQ
• 分子名称: Outer membrane protein assembly factor BamE, ZINC ION (3 entities in total)
• 機能のキーワード: beta-barrel assembly machinery, bam complex, lipoprotein, membrane protein
• 由来する生物種: Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 24332.88

構造登録者

Korotkov, K.V.,Buchanan, S.K.,Noinaj, N. (登録日: 2017-06-26, 公開日: 2017-12-06, 最終更新日: 2024-03-13)

主引用文献

Sikora, A.E.,Wierzbicki, I.H.,Zielke, R.A.,Ryner, R.F.,Korotkov, K.V.,Buchanan, S.K.,Noinaj, N.
Structural and functional insights into the role of BamD and BamE within the beta-barrel assembly machinery in Neisseria gonorrhoeae.
J. Biol. Chem., 293:1106-1119, 2018

PubMed Abstract: The β-barrel assembly machinery (BAM) is a conserved multicomponent protein complex responsible for the biogenesis of β-barrel outer membrane proteins (OMPs) in Gram-negative bacteria. Given its role in the production of OMPs for survival and pathogenesis, BAM represents an attractive target for the development of therapeutic interventions, including drugs and vaccines against multidrug-resistant bacteria such as The first structure of BamA, the central component of BAM, was from , the etiological agent of the sexually transmitted disease gonorrhea. To aid in pharmaceutical targeting of BAM, we expanded our studies to BamD and BamE within BAM of this clinically relevant human pathogen. We found that the presence of BamD, but not BamE, is essential for gonococcal viability. However, BamE, but not BamD, was cell-surface-displayed under native conditions; however, in the absence of BamE, BamD indeed becomes surface-exposed. Loss of BamE altered cell envelope composition, leading to slower growth and an increase in both antibiotic susceptibility and formation of membrane vesicles containing greater amounts of vaccine antigens. Both BamD and BamE are expressed in diverse gonococcal isolates, under host-relevant conditions, and throughout different phases of growth. The solved structures of BamD and BamE share overall folds with proteins but contain differences that may be important for function. Together, these studies highlight that, although BAM is conserved across Gram-negative bacteria, structural and functional differences do exist across species, which may be leveraged in the development of species-specific therapeutics in the effort to combat multidrug resistance.

PubMed: 29229778
DOI: 10.1074/jbc.RA117.000437

実験手法

X-RAY DIFFRACTION (2.45 Å)