Wie sekundäre Transporter mit substratbindenden Proteinen interagieren

Abstract

AbstractTRAP-transporters are widespread in bacteria and archaea and are often responsible for the transport of nutrients or virulence factors in pathogens. They consist of three domains, a substrate-binding protein and two membrane domains. Using cryo-EM, we have determined the structure of the membrane domains, revealing a monomeric elevator architecture. Further studies gave insights into the interaction between the domains of TRAP-transporters and how they can be specifically inhibited by using a VHH antibody.