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	The β-Grasp Domain of Proteasomal ATPase Mpa Makes Critical Contacts with the Mycobacterium tuberculosis 20S Core Particle to Facilitate Degradation.
Journal, issue, pages	mSphere, Vol. 7, Issue 5, Page e0027422, Year 2022
Publish date	Oct 26, 2022
Authors	Xiansha Xiao / Xiang Feng / Jin Hee Yoo / Amanda Kovach / K Heran Darwin / Huilin Li /
PubMed Abstract	Mycobacterium tuberculosis possesses a Pup-proteasome system analogous to the eukaryotic ubiquitin-proteasome pathway. We have previously shown that the hexameric mycobacterial proteasome ATPase (Mpa) ...Mycobacterium tuberculosis possesses a Pup-proteasome system analogous to the eukaryotic ubiquitin-proteasome pathway. We have previously shown that the hexameric mycobacterial proteasome ATPase (Mpa) recruits pupylated protein substrates via interactions between amino-terminal coiled-coils in Mpa monomers and the degradation tag Pup. However, it is unclear how Mpa rings interact with a proteasome due to the presence of a carboxyl-terminal β-grasp domain unique to Mpa homologues that makes the interaction highly unstable. Here, we describe newly identified critical interactions between Mpa and 20S core proteasomes. Interestingly, the Mpa C-terminal GQYL motif binds the 20S core particle activation pocket differently than the same motif of the ATP-independent proteasome accessory factor PafE. We further found that the β-hairpin of the Mpa β-grasp domain interacts variably with the H0 helix on top of the 20S core particle via a series of ionic and hydrogen-bond interactions. Individually mutating several involved residues reduced Mpa-mediated protein degradation both and . The Pup-proteasome system in Mycobacterium tuberculosis is critical for this species to cause lethal infections in mice. Investigating the molecular mechanism of how the Mpa ATPase recruits and unfolds pupylated substrates to the 20S proteasomal core particle for degradation will be essential to fully understand how degradation is regulated, and the structural information we report may be useful for the development of new tuberculosis chemotherapies.
External links	mSphere / PubMed:35993699 / PubMed Central
Methods	EM (single particle)
Resolution	3.0 - 10.0 Å
Structure data	27223 8d6v EMDB-27223: Cryo-EM 3D map of the Mycobacterium tuberculosis 20S proteasome bound to the C-terminal GQYL motif of the ATP-bound Mpa ATPase PDB-8d6v: Structure of the Mycobacterium tuberculosis 20S proteasome bound to the C-terminal GQYL motif of the ATP-bound Mpa ATPase Method: EM (single particle) / Resolution: 3.2 Å 27224 8d6w EMDB-27224: Cryo-EM 3D map of the Mycobacterium tuberculosis 20S proteasome bound to the C-terminal GQYL motif of the ADP-bound Mpa ATPase PDB-8d6w: Structure of the Mycobacterium tuberculosis 20S proteasome bound to the C-terminal GQYL motif of the ADP-bound Mpa ATPase Method: EM (single particle) / Resolution: 3.0 Å 27225 8d6x EMDB-27225: Cryo-EM 3D map of the Mycobacterium tuberculosis 20S proteasome bound to the ATP-bound Mpa ATPase PDB-8d6x: Structure of the Mycobacterium tuberculosis 20S proteasome bound to the ATP-bound Mpa ATPase Method: EM (single particle) / Resolution: 3.2 Å 27226 8d6y EMDB-27226: Cryo-EM 3D map of the Mycobacterium tuberculosis 20S proteasome bound to the ADP-bound Mpa ATPase PDB-8d6y: Structure of the Mycobacterium tuberculosis 20S proteasome bound to the ADP-bound Mpa ATPase Method: EM (single particle) / Resolution: 10.0 Å
Source	mycobacterium tuberculosis (bacteria)
Keywords	ANTIMICROBIAL PROTEIN / Mpa / proteasome