Protein oligomerization in the bacterial outer membrane (Review).

TitleProtein oligomerization in the bacterial outer membrane (Review).
Publication TypeJournal Article
Year of Publication2009
AuthorsMeng, G., R. Fronzes, V. Chandran, H. Remaut, and G. Waksman
JournalMol Membr Biol
Volume26
Issue3
Pagination136-45
Date Published2009 Apr
Type of Articlesmm
ISSN1464-5203
KeywordsBacterial Outer Membrane Proteins, Protein Conformation, Protein Multimerization
Abstract

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.

DOI10.1080/09687680802712422
Alternate JournalMol. Membr. Biol.
PubMed ID19225986
Grant List08087 / / Wellcome Trust / United Kingdom