Distortion of the bilayer and dynamics of the BAM complex in lipid nanodiscs
The result's identifiers
Result code in 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>
Result on the web
<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>
Alternative languages
Result language
angličtina
Original language name
Distortion of the bilayer and dynamics of the BAM complex in lipid nanodiscs
Original language description
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.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10608 - Biochemistry and molecular biology
Result continuities
Project
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Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2020
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Communications Biology
ISSN
2399-3642
e-ISSN
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Volume of the periodical
3
Issue of the periodical within the volume
1
Country of publishing house
US - UNITED STATES
Number of pages
14
Pages from-to
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UT code for WoS article
000599847000002
EID of the result in the Scopus database
2-s2.0-85098475705