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Cryo-EM study of Mycolicibacterium smegmatis membrane protein MmpL5S5

ABSTRACT: This is the proteomic analysis data of Mycolicibacterium smegmatis membrane protein MmpL5S5 subjected to cryo-EM study.

INSTRUMENT(S):

ORGANISM(S): Mycobacterium Smegmatis (strain Atcc 700084 / Mc(2)155)

SUBMITTER: zhemin zhang

LAB HEAD: Edward, W, Yu

PROVIDER: PXD060321 | Pride | 2025-08-25

REPOSITORIES: Pride

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Publications

Structures of MmpL complexes reveal the assembly and mechanism of this family of transporters.

Zhang Zhemin Z Maharjan Rakesh R Gregor William D WD Klenotic Philip A PA Yu Edward W EW

Science advances 20250813 33

We coexpressed the mycobacterial membrane protein large 5 (MmpL5) transporter and MmpS5 adaptor proteins in <i>Mycobacterium smegmatis</i> and defined their structures from detergent-solubilized crude membranes. We observed that MmpL5 presents as a monomer in complex with the cytosolic meromycolate extension acyl carrier protein M (AcpM), where these AcpM-MmpL5 complexes generate regular two-dimensional arrays. We also provide structural information to show that <i>M. smegmatis</i> MmpL5 assembl ...[more]

PMID: 40802754

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