Conformational flexibility of EptA driven by an interdomain helix provides insights for enzyme-substrate recognition.

ABSTRACT: Many pathogenic gram-negative bacteria have developed mechanisms to increase resistance to cationic antimicrobial peptides by modifying the lipid A moiety. One modification is the addition of phospho-ethano-lamine to lipid A by the enzyme phospho-ethano-lamine transferase (EptA). Previously we reported the structure of EptA from Neisseria, revealing a two-domain architecture consisting of a periplasmic facing soluble domain and a transmembrane domain, linked together by a bridging helix. Here, the conformational flexibility of EptA in different detergent environments is probed by solution scattering and intrinsic fluorescence-quenching studies. The solution scattering studies reveal the enzyme in a more compact state with the two domains positioned close together in an n-do-d

SUBMITTER: Anandan A 

PROVIDER: S-EPMC8420757 | biostudies-literature | 2021 Sep

REPOSITORIES: biostudies-literature