Protein oligomerization in the bacterial outer membrane (Review).
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.
Meng
Guoyu
G
Institute of Structural and Molecular Biology, University College London and Birkbeck College, London, UK.
Fronzes
Rémi
R
Chandran
Vidya
V
Remaut
Han
H
Waksman
Gabriel
G
D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry* / Q000502:physiology; D011487:Protein Conformation; D055503:Protein Multimerization
D001425:Bacterial Outer Membrane Proteins