7YE4
BAM-EspP complex structure with BamA-G431C and G781C/EspP-N1293C and A1043C mutations in nanodisc
7YE4 の概要
| エントリーDOI | 10.2210/pdb7ye4/pdb |
| 関連するPDBエントリー | 7XKL 7YD5 |
| EMDBエントリー | 33763 |
| 分子名称 | Outer membrane protein assembly factor BamA, Outer membrane protein assembly factor BamB, Outer membrane protein assembly factor BamC, ... (6 entities in total) |
| 機能のキーワード | bam, bamabcde, espp, gram-negative bacteria, outer membrane protein, outer membrane barrel, bama, bamb, bamc, bamd, bame, membrane protein |
| 由来する生物種 | Escherichia coli K-12 詳細 |
| タンパク質・核酸の鎖数 | 6 |
| 化学式量合計 | 249678.27 |
| 構造登録者 | |
| 主引用文献 | Shen, C.,Chang, S.,Luo, Q.,Chan, K.C.,Zhang, Z.,Luo, B.,Xie, T.,Lu, G.,Zhu, X.,Wei, X.,Dong, C.,Zhou, R.,Zhang, X.,Tang, X.,Dong, H. Structural basis of BAM-mediated outer membrane beta-barrel protein assembly. Nature, 617:185-193, 2023 Cited by PubMed Abstract: The outer membrane structure is common in Gram-negative bacteria, mitochondria and chloroplasts, and contains outer membrane β-barrel proteins (OMPs) that are essential interchange portals of materials. All known OMPs share the antiparallel β-strand topology, implicating a common evolutionary origin and conserved folding mechanism. Models have been proposed for bacterial β-barrel assembly machinery (BAM) to initiate OMP folding; however, mechanisms by which BAM proceeds to complete OMP assembly remain unclear. Here we report intermediate structures of BAM assembling an OMP substrate, EspP, demonstrating sequential conformational dynamics of BAM during the late stages of OMP assembly, which is further supported by molecular dynamics simulations. Mutagenic in vitro and in vivo assembly assays reveal functional residues of BamA and EspP for barrel hybridization, closure and release. Our work provides novel insights into the common mechanism of OMP assembly. PubMed: 37100902DOI: 10.1038/s41586-023-05988-8 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (3.4 Å) |
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