Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Structures of the β-barrel assembly machine recognizing outer membrane protein substrates.
Journal, issue, pages	FASEB J, Vol. 35, Issue 1, Page e21207, Year 2021
Publish date	Jun 15, 2021
Authors	Le Xiao / Long Han / Bufan Li / Manfeng Zhang / Haizhen Zhou / Qingshan Luo / Xinzheng Zhang / Yihua Huang /
PubMed Abstract	β-barrel outer membrane proteins (β-OMPs) play critical roles in nutrition acquisition, protein import/export, and other fundamental biological processes. The assembly of β-OMPs in Gram-negative ...β-barrel outer membrane proteins (β-OMPs) play critical roles in nutrition acquisition, protein import/export, and other fundamental biological processes. The assembly of β-OMPs in Gram-negative bacteria is mediated by the β-barrel assembly machinery (BAM) complex, yet its precise mechanism remains elusive. Here, we report two structures of the BAM complex in detergents and in nanodisks, and two crystal structures of the BAM complex with bound substrates. Structural analysis indicates that the membrane compositions surrounding the BAM complex could modulate its overall conformations, indicating low energy barriers between different conformational states and a highly dynamic nature of the BAM complex. Importantly, structures of the BAM complex with bound substrates and the related functional analysis show that the first β-strand of the BamA β-barrel (β1 ) in the BAM complex is associated with the last but not the first β-strand of a β-OMP substrate via antiparallel β-strand interactions. These observations are consistent with the β-signal hypothesis during β-OMP biogenesis, and suggest that the β1 strand in the BAM complex may interact with the last β-strand of an incoming β-OMP substrate upon their release from the chaperone-bound state.
External links	FASEB J / PubMed:33368572
Methods	EM (single particle) / X-ray diffraction
Resolution	3.05 - 4.2 Å
Structure data	30018 6lyu EMDB-30018, PDB-6lyu: Structure of the BAM complex Method: EM (single particle) / Resolution: 4.2 Å PDB-6lyq: Structure of the BAM complex Method: X-RAY DIFFRACTION / Resolution: 3.19 Å PDB-6lyr: Structure of the BAM complex Method: X-RAY DIFFRACTION / Resolution: 3.28 Å PDB-6lys: Structure of the BAM complex Method: X-RAY DIFFRACTION / Resolution: 3.05 Å
Source	escherichia coli k-12 (bacteria) escherichia coli (strain k12) (bacteria)
Keywords	MEMBRANE PROTEIN / b-barrel assembly machinery (BAM) complex