Structural basis for catalysis at the membrane-water interface.

Publication Type:

Journal Article

Authors:

Dufrisne, Meagan Belcher; Petrou, Vasileios I; Clarke, Oliver B; Mancia, Filippo

Source:

Biochim Biophys Acta Mol Cell Biol Lipids, Volume 1862, Issue 11, p.1368-1385 (2017)

Keywords:

Bacteria, Bacterial Proteins, Catalysis, Catalytic Domain, Cell Membrane, Hydrophobic and Hydrophilic Interactions, Membrane Lipids, Models, Molecular, Protein Conformation, alpha-Helical, Protein Conformation, beta-Strand, Protein Folding, Structure-Activity Relationship, Substrate Specificity, Water

Abstract:

<p>The membrane-water interface forms a uniquely heterogeneous and geometrically constrained environment for enzymatic catalysis. Integral membrane enzymes sample three environments - the uniformly hydrophobic interior of the membrane, the aqueous extramembrane region, and the fuzzy, amphipathic interfacial region formed by the tightly packed headgroups of the components of the lipid bilayer. Depending on the nature of the substrates and the location of the site of chemical modification, catalysis may occur in each of these environments. The availability of structural information for alpha-helical enzyme families from each of these classes, as well as several beta-barrel enzymes from the bacterial outer membrane, has allowed us to review here the different ways in which each enzyme fold has adapted to the nature of the substrates, products, and the unique environment of the membrane. Our focus here is on enzymes that process lipidic substrates. This article is part of a Special Issue entitled: Bacterial Lipids edited by Russell E. Bishop.</p>