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Curr Opin Struct Biol. 2011 Aug;21(4):523-31. doi: 10.1016/j.sbi.2011.05.005. Epub 2011 Jun 28.

The structural biology of β-barrel membrane proteins: a summary of recent reports.

Author information

1
National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892, USA.

Abstract

The outer membranes of Gram-negative bacteria, mitochondria, and chloroplasts all contain transmembrane β-barrel proteins. These β-barrel proteins serve essential functions in cargo transport and signaling and are also vital for membrane biogenesis. They have also been adapted to perform a diverse set of important cellular functions including acting as porins, transporters, enzymes, virulence factors and receptors. Recent structures of transmembrane β-barrels include that of a full length autotransporter (EstA), a bacterial heme transporter complex (HasR), a bacterial porin in complex with several ligands (PorB), and the mitochondrial voltage-dependent anion channel (VDAC) from both mouse and human. These represent only a few of the interesting structures of β-barrel membrane proteins recently elucidated. However, they demonstrate many of the advancements made within the field of transmembrane protein structure in the past few years.

PMID:
21719274
PMCID:
PMC3164749
DOI:
10.1016/j.sbi.2011.05.005
[Indexed for MEDLINE]
Free PMC Article

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