6IZT

Crystal structure of Haemophilus Influenzae BamA POTRA3-5

Summary for 6IZT

• Entry DOI: 10.2210/pdb6izt/pdb
• Descriptor: Outer membrane protein assembly factor BamA (2 entities in total)
• Functional Keywords: beta-barrel assembly machinery, poly-potras, omp recruitment, lipo-partners, transport protein
• Biological source: Haemophilus influenzae
• Total number of polymer chains: 2
• Total formula weight: 60132.88

Authors

Ma, X.,Wang, Q.,Li, Y.,Tan, P.,Wu, H.,Wang, P.,Dong, X.,Hong, L.,Meng, G. (deposition date: 2018-12-20, release date: 2019-10-30, Last modification date: 2023-11-22)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.03 Å)