Structure of a nascent membrane protein as it folds on the BAM complex.

Nature
David TomasekDaniel Kahne

Abstract

Mitochondria, chloroplasts and Gram-negative bacteria are encased in a double layer of membranes. The outer membrane contains proteins with a β-barrel structure1,2. β-Barrels are sheets of β-strands wrapped into a cylinder, in which the first strand is hydrogen-bonded to the final strand. Conserved multi-subunit molecular machines fold and insert these proteins into the outer membrane3-5. One subunit of the machines is itself a β-barrel protein that has a central role in folding other β-barrels. In Gram-negative bacteria, the β-barrel assembly machine (BAM) consists of the β-barrel protein BamA, and four lipoproteins5-8. To understand how the BAM complex accelerates folding without using exogenous energy (for example, ATP)9, we trapped folding intermediates on this machine. Here we report the structure of the BAM complex of Escherichia coli folding BamA itself. The BamA catalyst forms an asymmetric hybrid β-barrel with the BamA substrate. The N-terminal edge of the BamA catalyst has an antiparallel hydrogen-bonded interface with the C-terminal edge of the BamA substrate, consistent with previous crosslinking studies10-12; the other edges of the BamA catalyst and substrate are close to each other, but curl inward and do not pair...Continue Reading

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Citations

Jun 6, 2020·The Journal of Biological Chemistry·Jim E HorneSheena E Radford
Jul 18, 2020·Proceedings of the National Academy of Sciences of the United States of America·Elizabeth M HartThomas J Silhavy
Aug 21, 2020·Journal of Bacteriology·Elizabeth M Hart, Thomas J Silhavy
Dec 29, 2020·FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology·Le XiaoYihua Huang
Jan 6, 2021·Medicine in Drug Discovery·Gregory UpertPhilipp Ermert
Nov 18, 2020·Nature Chemical Biology·Francesco FiorentinoCarol V Robinson
Dec 15, 2020·Molecular Microbiology·Karl LundquistNicholas Noinaj
Feb 4, 2021·Trends in Cell Biology·Xudong Wu, Tom A Rapoport
Feb 10, 2021·Current Opinion in Microbiology·David Tomasek, Daniel Kahne
Mar 5, 2021·Current Opinion in Microbiology·Julia E Page, Suzanne Walker
Feb 28, 2021·Biochimica Et Biophysica Acta. Biomembranes·Xiaoyu ChenHsin-Hui Shen
Feb 28, 2021·Journal of Molecular Biology·Kathryn A DiederichsIstvan Botos
Mar 12, 2021·Molecular Cell·Matthew Thomas Doyle, Harris David Bernstein
Mar 17, 2021·Chemical Reviews·Jigneshkumar Dahyabhai PrajapatiMathias Winterhalter
Mar 22, 2021·The Journal of Biological Chemistry·Fei LiRobert M Stroud
Mar 31, 2021·Nature Structural & Molecular Biology·Xiaodi TangHaohao Dong
Apr 27, 2021·Current Opinion in Structural Biology·Jérémy Guérin, Susan K Buchanan
May 1, 2021·Journal of Industrial Microbiology & Biotechnology·Li CaoA James Link
Jun 3, 2021·Toxins·Nathalie Dautin
May 29, 2021·FEMS Microbiology Letters·Maurice SteenhuisJoen Luirink
Jul 9, 2021·Nature Communications·Paul WhiteSheena E Radford
Jul 22, 2021·Journal of Materials Chemistry. B, Materials for Biology and Medicine·Ya-Lin QiHai-Liang Zhu
Aug 6, 2021·Proceedings of the National Academy of Sciences of the United States of America·Muralidhar TataAnna Konovalova
Dec 2, 2021·ACS Synthetic Biology·Sol Vendrell-FernándezRafael Giraldo
Jan 1, 2022·Proceedings of the National Academy of Sciences of the United States of America·Ashton N Combs, Thomas J Silhavy
Oct 10, 2020·Biochimica Et Biophysica Acta. Bioenergetics·Arushi Gupta, Thomas Becker

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Methods Mentioned

BETA
X-ray
crosslinking studies
size-exclusion chromatography
electron microscopy

Software Mentioned

Chimera
MolProbity
PHENIX
SerialEM
TASSER
MotionCor2
PyMOL
Relion
Coot
CTFFIND4

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