Structural insight into the biogenesis of β-barrel membrane proteins

Nicholas Noinaj, Adam J. Kuszak, James C. Gumbart, Petra Lukacik, Hoshing Chang, Nicole C. Easley, Trevor Lithgow and Susan K. Buchanan ()
Additional contact information
Nicholas Noinaj: National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health
Adam J. Kuszak: National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health
James C. Gumbart: School of Physics, Georgia Institute of Technology
Petra Lukacik: Diamond Light Source Ltd, Oxfordshire OX11 0DE, UK
Hoshing Chang: National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health
Nicole C. Easley: National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health
Trevor Lithgow: Monash University, Victoria 3800, Australia
Susan K. Buchanan: National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health

Nature, 2013, vol. 501, issue 7467, 385-390

Abstract: 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.

Date: 2013
References: Add references at CitEc
Citations: View citations in EconPapers (2)

Downloads: (external link)
https://www.nature.com/articles/nature12521 Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:501:y:2013:i:7467:d:10.1038_nature12521

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/nature12521

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().