Journal
MOLECULAR MEMBRANE BIOLOGY
Volume 26, Issue 3, Pages 136-145Publisher
TAYLOR & FRANCIS LTD
DOI: 10.1080/09687680802712422
Keywords
Bacterial outer membrane; oligomerization; membrane protein; structural biology; beta-barrel
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Funding
- Wellcome Trust [08087]
- MRC [G0800002] Funding Source: UKRI
- Medical Research Council [G0800002] Funding Source: researchfish
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The formation of homo-oligomeric assemblies is a well-established characteristic of many soluble proteins and enzymes. Oligomerization has been shown to increase protein stability, allow allosteric cooperativity, shape reaction compartments and provide multivalent interaction sites in soluble proteins. In comparison, our understanding of the prevalence and reasons behind protein oligomerization in membrane proteins is relatively sparse. Recent progress in structural biology of bacterial outer membrane proteins has suggested that oligomerization may be as common and versatile as in soluble proteins. Here we review the current understanding of oligomerization in the bacterial outer membrane from a structural and functional point of view.
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