Chapter 11 Bacterial Membrane Proteins: The New Soluble Proteins?

Abstract

Publisher Summary In recent years, the successful structure determination of membrane proteins has become accelerated. Advances in protein production and crystallization have underpinned the structure determination of novel membrane proteins. The outer and inner membrane proteins of bacteria have been the most intensively studied. This chapter discusses the structure of outer membrane proteins (OMPs) and highlights the recent advances in protein production. OMPs have a variety of different functions, but, at their core, they allow compounds in and out the cell. OMPs are relatively easy to produce and crystallize, and this has resulted in the publication of many studies. The defining characteristic of these proteins is the β-barrel transmembrane region. It has been assumed that all OMPs are β-barrels. The publication of the first α-helical OMPs, Wza shows this is not the case. The structural determination of eukaryotic integral and bacterial inner membrane proteins has been more challenging. In most cases, the production of stable protein has been the principal difficulty. Several research groups have developed new technologies to overcome these challenges. This chapter highlights some of the most recent ones. The advances in protein production and crystallization technology also resulted in the long sought structure of human G-protein coupled receptors (GPCR).