| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1979335 | Current Opinion in Structural Biology | 2011 | 9 Pages |
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.
► We provide an introduction to β-barrel proteins. ► We review the structures of three bacterial outer membrane proteins. ► We review the recent structures of VDAC. ► We provide links to useful online databases for β-barrel proteins. ► We summarize the current field of β-barrel transmembrane proteins and provide our opinion about the future.
