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 and dynamics of a mycobacterial type VII secretion system.
Journal, issue, pages	Nature, Vol. 593, Issue 7859, Page 445-448, Year 2021
Publish date	May 12, 2021
Authors	Catalin M Bunduc / Dirk Fahrenkamp / Jiri Wald / Roy Ummels / Wilbert Bitter / Edith N G Houben / Thomas C Marlovits /
PubMed Abstract	Mycobacterium tuberculosis is the cause of one of the most important infectious diseases in humans, which leads to 1.4 million deaths every year. Specialized protein transport systems-known as ...Mycobacterium tuberculosis is the cause of one of the most important infectious diseases in humans, which leads to 1.4 million deaths every year. Specialized protein transport systems-known as type VII secretion systems (T7SSs)-are central to the virulence of this pathogen, and are also crucial for nutrient and metabolite transport across the mycobacterial cell envelope. Here we present the structure of an intact T7SS inner-membrane complex of M. tuberculosis. We show how the 2.32-MDa ESX-5 assembly, which contains 165 transmembrane helices, is restructured and stabilized as a trimer of dimers by the MycP protease. A trimer of MycP caps a central periplasmic dome-like chamber that is formed by three EccB dimers, with the proteolytic sites of MycP facing towards the cavity. This chamber suggests a central secretion and processing conduit. Complexes without MycP show disruption of the EccB periplasmic assembly and increased flexibility, which highlights the importance of MycP for complex integrity. Beneath the EccB-MycP chamber, dimers of the EccC ATPase assemble into three bundles of four transmembrane helices each, which together seal the potential central secretion channel. Individual cytoplasmic EccC domains adopt two distinctive conformations that probably reflect different secretion states. Our work suggests a previously undescribed mechanism of protein transport and provides a structural scaffold to aid in the development of drugs against this major human pathogen.
External links	Nature / PubMed:33981042 / PubMed Central
Methods	EM (single particle)
Resolution	3.27 - 7.58 Å
Structure data	12514 7np7 EMDB-12514: Structure of an intact ESX-5 inner membrane complex, C1 symmetry PDB-7np7: Structure of an intact ESX-5 inner membrane complex, Composite C1 model Method: EM (single particle) / Resolution: 4.03 Å 12517 7npr EMDB-12517: Structure of an intact ESX-5 inner membrane complex, C3 symmetry PDB-7npr: Structure of an intact ESX-5 inner membrane complex, Composite C3 model Method: EM (single particle) / Resolution: 3.82 Å 12518 7nps EMDB-12518: Structure of the periplasmic assembly from the ESX-5 inner membrane complex, C1 symmetry PDB-7nps: Structure of the periplasmic assembly from the ESX-5 inner membrane complex, C1 model Method: EM (single particle) / Resolution: 3.81 Å EMDB-12519: Periplasmic assembly of the intact ESX-5 inner membrane complex, C3 symmetry Method: EM (single particle) / Resolution: 3.52 Å 12520 7npt EMDB-12520, PDB-7npt: Cytosolic bridge of an intact ESX-5 inner membrane complex Method: EM (single particle) / Resolution: 3.27 Å 12521 7npu EMDB-12521, PDB-7npu: MycP5-free ESX-5 inner membrane complex, state I Method: EM (single particle) / Resolution: 4.48 Å 12522 7npv EMDB-12522, PDB-7npv: MycP5-free ESX-5 inner membrane complex, State II Method: EM (single particle) / Resolution: 6.66 Å EMDB-12523: Structure of an intact ESX-5 inner membrane complex, EccC5 extended Method: EM (single particle) / Resolution: 4.27 Å EMDB-12525: Structure of an intact ESX-5 inner membrane complex, EccC contracted Method: EM (single particle) / Resolution: 7.58 Å
Source	Mycobacterium tuberculosis H37Rv (bacteria) mycobacterium tuberculosis (strain atcc 25618 / h37rv) (bacteria)
Keywords	MEMBRANE PROTEIN / T7SS / mycobacteria / protein transport / secretion / type VII secretion system / membrane