Cryo-EM structure of the Mycobacterium smegmatis MmpL5-AcpM complex.

ABSTRACT: Mycobacterium tuberculosis, the causative agent of the airborne infection tuberculosis (TB), contains 13 mycobacterial membrane protein large (MmpL) transporters that can be divided into two distinct subclasses. These MmpL proteins play important functional roles within the mycobacterium and subsequently are considered attractive drug targets to combat TB infection. Previously, we reported both X-ray and cryo-electron microscopy (cryo-EM) structures of the MmpL3 transporter, providing high-resolution structural information for this subclass of the MmpL proteins. Thus far, there is no structural information available for the other subclass, which includes MmpL5, an inner membrane transporter that plays a critical role in iron hemostasis. Here, we report the first cryo-EM structure of

SUBMITTER: Maharjan R 

PROVIDER: S-EPMC11633376 | biostudies-literature | 2024 Dec

REPOSITORIES: biostudies-literature