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Cited by 431

The DOI matches its Crossref record; 58 of the 58 references it cites were found in a registry or an index.

Structural insight into the biogenesis of β-barrel membrane proteins

Open access
Noinaj, Nicholas, Kuszak, Adam J., Gumbart, James C., Lukacik, Petra, Chang, Hoshing, Easley, Nicole C., Lithgow, Trevor, Buchanan, Susan K.·2013·Nature

Abstract

β-barrel membrane proteins are essential for nutrient import, signalling, motility and survival. In Gram-negative bacteria, the β-barrel assembly machinery (BAM) complex is responsible for the biogenesis of β-barrel membrane proteins, with homologous complexes found in mitochondria and chloroplasts. Here we describe the structure of BamA, the central and essential component of the BAM complex, from two species of bacteria: Neisseria gonorrhoeae and Haemophilus ducreyi. BamA consists of a large periplasmic domain attached to a 16-strand transmembrane β-barrel domain. Three structural features shed light on the mechanism by which BamA catalyses β-barrel assembly. First, the interior cavity is accessible in one BamA structure and conformationally closed in the other. Second, an exterior rim of the β-barrel has a distinctly narrowed hydrophobic surface, locally destabilizing the outer membrane. And third, the β-barrel can undergo lateral opening, suggesting a route from the interior cavity in BamA into the outer membrane.

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Metadata

Authors
Noinaj, N., Kuszak, A. J., Gumbart, J. C., Lukacik, P., Chang, H., Easley, N. C., Lithgow, T., & Buchanan, S. K.
Venue
Nature
Published
2013-09-01
Volume
501
Issue
7467
Pages
385-390
ISSN
  • 0028-0836 (ISSN-L)
  • 1476-4687
OpenAlex
W2060719766
Cited by
431
References
58
FWCI
32.17
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Structural insight into the biogenesis of β-barrel membrane proteins. https://app.cochat.ai/papers/10.1038/nature12521
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Noinaj, N., Kuszak, A. J., Gumbart, J. C., Lukacik, P., Chang, H., Easley, N. C., Lithgow, T., & Buchanan, S. K. (2013). Structural insight into the biogenesis of β-barrel membrane proteins. Nature. https://doi.org/10.1038/nature12521

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