6IZS

Crystal structure of Haemophilus influenzae BamA POTRA4

6IZS の概要

• エントリーDOI: 10.2210/pdb6izs/pdb
• 分子名称: Outer membrane protein assembly factor BamA (2 entities in total)
• 機能のキーワード: beta-barrel assembly machinery, poly-potras, omp recruitment, lipo-partners, transport protein
• 由来する生物種: Haemophilus influenzae
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12906.37

構造登録者

Ma, X.,Wang, Q.,Li, Y.,Tan, P.,Wu, H.,Wang, P.,Dong, X.,Hong, L.,Meng, G. (登録日: 2018-12-20, 公開日: 2019-10-30, 最終更新日: 2023-11-22)

主引用文献

Ma, X.,Wang, Q.,Li, Y.,Tan, P.,Wu, H.,Wang, P.,Dong, X.,Hong, L.,Meng, G.
How BamA recruits OMP substratesviapoly-POTRAs domain.
Faseb J., 33:14690-14702, 2019

PubMed Abstract: Almost all the outer membrane proteins (OMPs) fold into an invariant β-barrel fold the polypeptide-transport-associated (POTRA) motif and β-barrel assembly machinery (BAM). However, whether and how poly-POTRAs interact with OMPs remain largely unknown. Here, we have characterized the structures of poly-POTRAs X-ray crystallography, small angle X-ray scattering, and molecular dynamics simulation. Unexpectedly, crystal packing reveals a putative OMP travel pathway spiraled by the conserved α2-β2 edges in poly-POTRAs. Supportively, the structure-based mutations targeting the OMP binding sites significantly disrupt OMP biogenesis, resulting in severe cell growth defects. Another notable feature in POTRA structures is flexibility. As characterized by ELISA assays, poly-POTRAs could recruit OMP substrates in a step-wise manner. More importantly, the restriction of POTRA-POTRA linkage and flexibility significantly impairs the BamA function and causes cell growth defect. Altogether, these results suggest that the β-strand augmentations and intrinsic flexibility are important factors for BamA-OMP recruitment.-Ma, X., Wang, Q., Li, Y., Tan, P., Wu, H., Wang, P., Dong, X., Hong, L., Meng, G. How BamA recruits OMP substrates poly-POTRAs domain.

PubMed: 31702961
DOI: 10.1096/fj.201900681RR

実験手法

X-RAY DIFFRACTION (2.03 Å)