Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Structure of an endogenous mycobacterial MCE lipid transporter.
Journal, issue, pages	Nature, Vol. 620, Issue 7973, Page 445-452, Year 2023
Publish date	Jul 26, 2023
Authors	James Chen / Alice Fruhauf / Catherine Fan / Jackeline Ponce / Beatrix Ueberheide / Gira Bhabha / Damian C Ekiert /
PubMed Abstract	To replicate inside macrophages and cause tuberculosis, Mycobacterium tuberculosis must scavenge a variety of nutrients from the host. The mammalian cell entry (MCE) proteins are important virulence ...To replicate inside macrophages and cause tuberculosis, Mycobacterium tuberculosis must scavenge a variety of nutrients from the host. The mammalian cell entry (MCE) proteins are important virulence factors in M. tuberculosis, where they are encoded by large gene clusters and have been implicated in the transport of fatty acids and cholesterol across the impermeable mycobacterial cell envelope. Very little is known about how cargos are transported across this barrier, and it remains unclear how the approximately ten proteins encoded by a mycobacterial mce gene cluster assemble to transport cargo across the cell envelope. Here we report the cryo-electron microscopy (cryo-EM) structure of the endogenous Mce1 lipid-import machine of Mycobacterium smegmatis-a non-pathogenic relative of M. tuberculosis. The structure reveals how the proteins of the Mce1 system assemble to form an elongated ABC transporter complex that is long enough to span the cell envelope. The Mce1 complex is dominated by a curved, needle-like domain that appears to be unrelated to previously described protein structures, and creates a protected hydrophobic pathway for lipid transport across the periplasm. Our structural data revealed the presence of a subunit of the Mce1 complex, which we identified using a combination of cryo-EM and AlphaFold2, and name LucB. Our data lead to a structural model for Mce1-mediated lipid import across the mycobacterial cell envelope.
External links	Nature / PubMed:37495693
Methods	EM (single particle)
Resolution	2.71 - 3.19 Å
Structure data	29023 8fed EMDB-29023, PDB-8fed: Structure of Mce1-LucB complex from Mycobacterium smegmatis (Map1) Method: EM (single particle) / Resolution: 2.76 Å 29024 8fee EMDB-29024, PDB-8fee: Structure of Mce1 transporter from Mycobacterium smegmatis in the absence of LucB (Map2) Method: EM (single particle) / Resolution: 2.9 Å 29025 8fef EMDB-29025, PDB-8fef: Structure of Mce1 transporter from Mycobacterium smegmatis (Map0) Method: EM (single particle) / Resolution: 2.71 Å EMDB-29228: Local refinement of MceG in Msmeg Mce1 transporter (Map0a) Method: EM (single particle) / Resolution: 2.91 Å EMDB-29229: Local refinement of YrbE and MCE ring in Msmeg Mce1 transporter (Map0b) Method: EM (single particle) / Resolution: 2.73 Å EMDB-29230: Local refinement of MCE ring and needle in Msmeg Mce1 transporter (Map0c) Method: EM (single particle) / Resolution: 2.75 Å EMDB-29231: Local refinement of MCE needle and portal in Msmeg Mce1 transporter (Map0d) Method: EM (single particle) / Resolution: 3.0 Å EMDB-29232: Raw, consensus refinement of Msmeg Mce1 transporter (Map0e) Method: EM (single particle) / Resolution: 2.92 Å EMDB-29233: Local refinement of MceG in Msmeg Mce1-LucB complex (Map1a) Method: EM (single particle) / Resolution: 3.05 Å EMDB-29234: Local refinement of YrbE, MCE ring, LucB in Msmeg Mce1-LucB complex (Map1b) Method: EM (single particle) / Resolution: 2.89 Å EMDB-29235: Local refinement of MCE ring and needle in Msmeg Mce1-LucB complex (Map1c) Method: EM (single particle) / Resolution: 2.97 Å EMDB-29236: Local refinement of MCE needle and portal in Msmeg Mce1-LucB complex (Map1d) Method: EM (single particle) / Resolution: 3.16 Å EMDB-29237: Raw, consensus refinement of Msmeg Mce1-LucB complex (Map1e) Method: EM (single particle) / Resolution: 3.04 Å EMDB-29238: Local refinement of MceG in Msmeg Mce1 transporter in the absence of LucB (Map2a) Method: EM (single particle) / Resolution: 3.13 Å EMDB-29239: Local refinement of YrbE and MCE ring in Msmeg Mce1 transporter in the absence of LucB (Map2b) Method: EM (single particle) / Resolution: 2.99 Å EMDB-29240: Local refinement of MCE ring and needle in Msmeg Mce1 transporter in the absence of LucB (Map2c) Method: EM (single particle) / Resolution: 3.06 Å EMDB-29241: Local refinement of MCE needle and portal in Msmeg Mce1 transporter in the absence of LucB (Map2d) Method: EM (single particle) / Resolution: 3.19 Å EMDB-29242: Raw, consensus refinement of Msmeg Mce1 transporter in the absence of LucB (Map2e) Method: EM (single particle) / Resolution: 3.1 Å
Chemicals	ChemComp, No image ChemComp-UNL: Unknown ligand
Source	mycolicibacterium smegmatis mc2 155 (bacteria)
Keywords	MEMBRANE PROTEIN / Membrane protein complex / ABC transporter / Virulence factor / Lipid transport