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Protein oligomerization in the bacterial outer membrane

Meng, GY; Fronzes, R; Chandran, V; Remaut, H; Waksman, G; (2009) Protein oligomerization in the bacterial outer membrane. MOL MEMBR BIOL , 26 (3) 136 - 145. 10.1080/09687680802712422.

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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.

Type: Article
Title: Protein oligomerization in the bacterial outer membrane
DOI: 10.1080/09687680802712422
Keywords: Bacterial outer membrane, oligomerization, membrane protein, structural biology, beta-barrel, GRAM-NEGATIVE BACTERIA, INFLUENZAE HIA AUTOTRANSPORTER, GENERAL SECRETORY PATHWAY, CHAPERONE-LIKE PROTEIN, ESCHERICHIA-COLI, CRYSTAL-STRUCTURE, STRUCTURAL BASIS, PHOSPHOLIPASE-A, PSEUDOMONAS-AERUGINOSA, TRANSLOCATOR DOMAIN
UCL classification: UCL > Provost and Vice Provost Offices
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Div of Biosciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Div of Biosciences > Structural and Molecular Biology
URI: http://discovery.ucl.ac.uk/id/eprint/168483
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