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

ABSTRACT: The outer membranes of Gram-negative bacteria, mitochondria, and chloroplasts all contain transmembrane ?-barrel proteins. These ?-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 ?-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 ?-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.

SUBMITTER: Fairman JW

PROVIDER: S-EPMC3164749 | biostudies-literature | 2011 Aug

REPOSITORIES: biostudies-literature

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

Fairman James W JW Noinaj Nicholas N Buchanan Susan K SK

Current opinion in structural biology 20110628 4

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 autotr ...[more]

PMID: 21719274

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