Distortion of the bilayer and dynamics of the BAM complex in lipid nanodiscs
Identifikátory výsledku
Kód výsledku v IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60076658%3A12310%2F20%3A43901449" target="_blank" >RIV/60076658:12310/20:43901449 - isvavai.cz</a>
Výsledek na webu
<a href="https://www.nature.com/articles/s42003-020-01419-w" target="_blank" >https://www.nature.com/articles/s42003-020-01419-w</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1038/s42003-020-01419-w" target="_blank" >10.1038/s42003-020-01419-w</a>
Alternativní jazyky
Jazyk výsledku
angličtina
Název v původním jazyce
Distortion of the bilayer and dynamics of the BAM complex in lipid nanodiscs
Popis výsledku v původním jazyce
The beta -barrel assembly machinery (BAM) catalyses the folding and insertion of beta -barrel outer membrane proteins (OMPs) into the outer membranes of Gram-negative bacteria by mechanisms that remain unclear. Here, we present an ensemble of cryoEM structures of the E. coli BamABCDE (BAM) complex in lipid nanodiscs, determined using multi-body refinement techniques. These structures, supported by single-molecule FRET measurements, describe a range of motions in the BAM complex, mostly localised within the periplasmic region of the major subunit BamA. The beta -barrel domain of BamA is in a 'lateral open' conformation in all of the determined structures, suggesting that this is the most energetically favourable species in this bilayer. Strikingly, the BAM-containing lipid nanodisc is deformed, especially around BAM's lateral gate. This distortion is also captured in molecular dynamics simulations, and provides direct structural evidence for the lipid 'disruptase' activity of BAM, suggested to be an important part of its functional mechanism. With cryo-EM, single-molecule FRET and MD simulations, Iadanza et al. characterise the membrane protein insertase complex BAM in lipid bilayer nanodiscs. They show that the beta -barrel domain of BamA is in a 'lateral open' conformation, and that BAM-containing lipid nanodisc deform around BAM's lateral gate, giving structural evidence for lipid 'disruptase' activity of BAM.
Název v anglickém jazyce
Distortion of the bilayer and dynamics of the BAM complex in lipid nanodiscs
Popis výsledku anglicky
The beta -barrel assembly machinery (BAM) catalyses the folding and insertion of beta -barrel outer membrane proteins (OMPs) into the outer membranes of Gram-negative bacteria by mechanisms that remain unclear. Here, we present an ensemble of cryoEM structures of the E. coli BamABCDE (BAM) complex in lipid nanodiscs, determined using multi-body refinement techniques. These structures, supported by single-molecule FRET measurements, describe a range of motions in the BAM complex, mostly localised within the periplasmic region of the major subunit BamA. The beta -barrel domain of BamA is in a 'lateral open' conformation in all of the determined structures, suggesting that this is the most energetically favourable species in this bilayer. Strikingly, the BAM-containing lipid nanodisc is deformed, especially around BAM's lateral gate. This distortion is also captured in molecular dynamics simulations, and provides direct structural evidence for the lipid 'disruptase' activity of BAM, suggested to be an important part of its functional mechanism. With cryo-EM, single-molecule FRET and MD simulations, Iadanza et al. characterise the membrane protein insertase complex BAM in lipid bilayer nanodiscs. They show that the beta -barrel domain of BamA is in a 'lateral open' conformation, and that BAM-containing lipid nanodisc deform around BAM's lateral gate, giving structural evidence for lipid 'disruptase' activity of BAM.
Klasifikace
Druh
J<sub>imp</sub> - Článek v periodiku v databázi Web of Science
CEP obor
—
OECD FORD obor
10608 - Biochemistry and molecular biology
Návaznosti výsledku
Projekt
—
Návaznosti
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Ostatní
Rok uplatnění
2020
Kód důvěrnosti údajů
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Údaje specifické pro druh výsledku
Název periodika
Communications Biology
ISSN
2399-3642
e-ISSN
—
Svazek periodika
3
Číslo periodika v rámci svazku
1
Stát vydavatele periodika
US - Spojené státy americké
Počet stran výsledku
14
Strana od-do
—
Kód UT WoS článku
000599847000002
EID výsledku v databázi Scopus
2-s2.0-85098475705