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	Cryo-EM structures reveal multiple stages of bacterial outer membrane protein folding.
Journal, issue, pages	Cell, Vol. 185, Issue 7, Page 1143-1156.e13, Year 2022
Publish date	Mar 31, 2022
Authors	Matthew Thomas Doyle / John R Jimah / Tyrone Dowdy / Shannon I Ohlemacher / Mioara Larion / Jenny E Hinshaw / Harris D Bernstein /
PubMed Abstract	Transmembrane β barrel proteins are folded into the outer membrane (OM) of Gram-negative bacteria by the β barrel assembly machinery (BAM) via a poorly understood process that occurs without known ...Transmembrane β barrel proteins are folded into the outer membrane (OM) of Gram-negative bacteria by the β barrel assembly machinery (BAM) via a poorly understood process that occurs without known external energy sources. Here, we used single-particle cryo-EM to visualize the folding dynamics of a model β barrel protein (EspP) by BAM. We found that BAM binds the highly conserved "β signal" motif of EspP to correctly orient β strands in the OM during folding. We also found that the folding of EspP proceeds via "hybrid-barrel" intermediates in which membrane integrated β sheets are attached to the essential BAM subunit, BamA. The structures show an unprecedented deflection of the membrane surrounding the EspP intermediates and suggest that β sheets progressively fold toward BamA to form a β barrel. Along with in vivo experiments that tracked β barrel folding while the OM tension was modified, our results support a model in which BAM harnesses OM elasticity to accelerate β barrel folding.
External links	Cell / PubMed:35294859 / PubMed Central
Methods	EM (single particle)
Resolution	3.6 - 4.8 Å
Structure data	26105 7tsz EMDB-26105, PDB-7tsz: BamABCDE bound to substrate EspP class 1 Method: EM (single particle) / Resolution: 4.5 Å 26106 7tt0 EMDB-26106, PDB-7tt0: BamABCDE bound to substrate EspP class 2 Method: EM (single particle) / Resolution: 4.3 Å 26107 7tt1 EMDB-26107, PDB-7tt1: BamABCDE bound to substrate EspP class 4 Method: EM (single particle) / Resolution: 4.3 Å 26108 7tt2 EMDB-26108, PDB-7tt2: BamABCDE bound to substrate EspP class 3 Method: EM (single particle) / Resolution: 4.2 Å 26109 7tt3 EMDB-26109, PDB-7tt3: BamABCDE bound to substrate EspP class 5 Method: EM (single particle) / Resolution: 4.3 Å 26110 7tt4 EMDB-26110, PDB-7tt4: BamABCDE bound to substrate EspP class 6 Method: EM (single particle) / Resolution: 4.2 Å 26111 7tt5 EMDB-26111, PDB-7tt5: BamABCDE bound to substrate EspP in the open-sheet EspP state Method: EM (single particle) / Resolution: 4.3 Å 26112 7tt6 EMDB-26112, PDB-7tt6: BamABCDE bound to substrate EspP in the intermediate-open EspP state Method: EM (single particle) / Resolution: 4.3 Å 26113 7tt7 EMDB-26113, PDB-7tt7: BamABCDE bound to substrate EspP in the barrelized EspP/continuous open BamA state Method: EM (single particle) / Resolution: 4.8 Å 26114 7ttc EMDB-26114, PDB-7ttc: BamABCDE bound to substrate EspP Method: EM (single particle) / Resolution: 3.6 Å
Chemicals	ChemComp-K33: 2,3-dideoxy-6-O-[2-deoxy-4-O-phosphono-2-(tetradecanoylamino)-alpha-L-gulopyranosyl]-1-O-phosphono-beta-D-threo-hexopyranose
Source	escherichia coli (E. coli)
Keywords	MEMBRANE PROTEIN / membrane protein folding / membrane dynamics / outer membrane protein / BAM / beta-barrel