Hydrogen-deuterium exchange reveals long-range dynamical allostery in soybean lipoxygenase.

ABSTRACT: In lipoxygenases, the topologically conserved C-terminal domain catalyzes the oxidation of polyunsaturated fatty acids, generating an assortment of biologically relevant signaling mediators. Plant and animal lipoxygenases also contain a 100-150-amino acid N-terminal C2-like domain that has been implicated in interactions with isolated fatty acids and at the phospholipid bilayer. These interactions may lead to increased substrate availability and contribute to the regulation of active-site catalysis. Because of a lack of structural information, a molecular understanding of this lipid-protein interaction remains unresolved. Herein, we employed hydrogen-deuterium exchange MS (HDXMS) to spatially resolve changes in protein conformation upon interaction of soybean lipoxygenase with a fatty acid

SUBMITTER: Offenbacher AR 

PROVIDER: S-EPMC5787793 | biostudies-literature | 2018 Jan

REPOSITORIES: biostudies-literature