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	Structural basis for allosteric modulation of M. tuberculosis proteasome core particle.
Journal, issue, pages	Nat Commun, Vol. 16, Issue 1, Page 3138, Year 2025
Publish date	Apr 1, 2025
Authors	Madison Turner / Adwaith B Uday / Algirdas Velyvis / Enrico Rennella / Natalie Zeytuni / Siavash Vahidi /
PubMed Abstract	The Mycobacterium tuberculosis (Mtb) proteasome system selectively degrades damaged or misfolded proteins and is crucial for the pathogen's survival within the host. Targeting the 20S core particle ...The Mycobacterium tuberculosis (Mtb) proteasome system selectively degrades damaged or misfolded proteins and is crucial for the pathogen's survival within the host. Targeting the 20S core particle (CP) offers a viable strategy for developing tuberculosis treatments. The activity of Mtb 20S CP, like that of its eukaryotic counterpart, is allosterically regulated, yet the specific conformations involved have not been captured in high-resolution structures to date. Here, we use single-particle electron cryomicroscopy and H/D exchange mass spectrometry to determine the Mtb 20S CP structure in an auto-inhibited state that is distinguished from the canonical resting state by the conformation of switch helices at the α/β interface. The rearrangement of these helices collapses the S1 pocket, effectively inhibiting substrate binding. Biochemical experiments show that the Mtb 20S CP activity can be altered through allosteric sites far from the active site. Our findings underscore the potential of targeting allostery to develop antituberculosis therapeutics.
External links	Nat Commun / PubMed:40169579 / PubMed Central
Methods	EM (single particle)
Resolution	2.5 - 2.89 Å
Structure data	45494 9ce5 EMDB-45494, PDB-9ce5: 20S Proteasome core particle Method: EM (single particle) / Resolution: 2.66 Å 45495 9ce7 EMDB-45495, PDB-9ce7: 20S Proteasome core particle open gate variant Method: EM (single particle) / Resolution: 2.72 Å 45496 9ce8 EMDB-45496, PDB-9ce8: 20S Proteasome core particle in complex with Ixazomib Method: EM (single particle) / Resolution: 2.61 Å 45498 9ceb EMDB-45498, PDB-9ceb: 20S Proteasome core particle beta-T1A mutant Method: EM (single particle) / Resolution: 2.5 Å 45499 9cee EMDB-45499, PDB-9cee: 20S Proteasome core particle beta-T1A mutant auto-inhibited state (Frame 1) Method: EM (single particle) / Resolution: 2.89 Å 45501 9ceg EMDB-45501, PDB-9ceg: 20S Proteasome core particle beta-T1A mutant resting state (Frame 20) Method: EM (single particle) / Resolution: 2.86 Å EMDB-45532: 20S proteasome core particle beta-T1A mutant intermediate frame 2 Method: EM (single particle) / Resolution: 2.83 Å EMDB-45534: 20S Proteasome core particle beta-T1A mutant intermediate frame 3 Method: EM (single particle) / Resolution: 2.8 Å EMDB-45535: 20S Proteasome core particle beta-T1A mutant intermediate frame 4 Method: EM (single particle) / Resolution: 2.78 Å EMDB-45537: 20S Proteasome core particle beta-T1A mutant intermediate frame 5 Method: EM (single particle) / Resolution: 2.74 Å EMDB-45538: 20S Proteasome core particle beta-T1A mutant intermediate frame 6 Method: EM (single particle) / Resolution: 2.73 Å EMDB-45539: 20S Proteasome core particle beta-T1A mutant intermediate frame 7 Method: EM (single particle) / Resolution: 2.71 Å EMDB-45540: 20S Proteasome core particle beta-T1A mutant intermediate frame 8 Method: EM (single particle) / Resolution: 2.7 Å EMDB-45541: 20S Proteasome core particle beta-T1A mutant intermediate frame 9 Method: EM (single particle) / Resolution: 2.73 Å EMDB-45542: 20S Proteasome core particle beta-T1A mutant intermediate frame 10 Method: EM (single particle) / Resolution: 2.68 Å EMDB-45547: 20S Proteasome core particle beta-T1A mutant intermediate frame 11 Method: EM (single particle) / Resolution: 2.76 Å EMDB-45552: 20S Proteasome core particle beta-T1A mutant intermediate frame 12 Method: EM (single particle) / Resolution: 2.7 Å EMDB-45553: 20S Proteasome core particle beta-T1A mutant intermediate frame 13 Method: EM (single particle) / Resolution: 2.7 Å EMDB-45556: 20S Proteasome core particle beta-T1A mutant intermediate frame 14 Method: EM (single particle) / Resolution: 2.74 Å EMDB-45558: 20S Proteasome core particle beta-T1A mutant intermediate frame 15 Method: EM (single particle) / Resolution: 2.75 Å EMDB-45559: 20S Proteasome core particle beta-T1A mutant intermediate frame 16 Method: EM (single particle) / Resolution: 2.76 Å EMDB-45560: 20S Proteasome core particle beta-T1A mutant intermediate frame 17 Method: EM (single particle) / Resolution: 2.79 Å EMDB-45561: 20S Proteasome core particle beta-T1A mutant intermediate frame 18 Method: EM (single particle) / Resolution: 2.81 Å EMDB-45562: 20S Proteasome core particle beta-T1A mutant intermediate frame 19 Method: EM (single particle) / Resolution: 2.82 Å
Chemicals	ChemComp-6V8: [(1~{R})-1-[2-[[2,5-bis(chloranyl)phenyl]carbonylamino]ethanoylamino]-3-methyl-butyl]boronic acid
Source	mycobacterium tuberculosis (bacteria)
Keywords	ANTIMICROBIAL PROTEIN / Proteasome / Proteolysis