7PXB

Substrate-engaged mycobacterial Proteasome-associated ATPase - focused 3D refinement (state B)


Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Resolution: 4.00 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

wwPDB Validation   3D Report Full Report


This is version 1.1 of the entry. See complete history


Literature

Structural basis of prokaryotic ubiquitin-like protein engagement and translocation by the mycobacterial Mpa-proteasome complex.

Kavalchuk, M.Jomaa, A.Muller, A.U.Weber-Ban, E.

(2022) Nat Commun 13: 276-276

  • DOI: 10.1038/s41467-021-27787-3
  • Primary Citation of Related Structures:  
    7PX9, 7PXA, 7PXB, 7PXC, 7PXD

  • PubMed Abstract: 
  • Proteasomes are present in eukaryotes, archaea and Actinobacteria, including the human pathogen Mycobacterium tuberculosis, where proteasomal degradation supports persistence inside the host. In mycobacteria and other members of Actinobacteria, prokaryotic ubiquitin-like protein (Pup) serves as a degradation tag post-translationally conjugated to target proteins for their recruitment to the mycobacterial proteasome ATPase (Mpa) ...

    Proteasomes are present in eukaryotes, archaea and Actinobacteria, including the human pathogen Mycobacterium tuberculosis, where proteasomal degradation supports persistence inside the host. In mycobacteria and other members of Actinobacteria, prokaryotic ubiquitin-like protein (Pup) serves as a degradation tag post-translationally conjugated to target proteins for their recruitment to the mycobacterial proteasome ATPase (Mpa). Here, we use single-particle cryo-electron microscopy to determine the structure of Mpa in complex with the 20S core particle at an early stage of pupylated substrate recruitment, shedding light on the mechanism of substrate translocation. Two conformational states of Mpa show how substrate is translocated stepwise towards the degradation chamber of the proteasome core particle. We also demonstrate, in vitro and in vivo, the importance of a structural feature in Mpa that allows formation of alternating charge-complementary interactions with the proteasome resulting in radial, rail-guided movements during the ATPase conformational cycle.


    Organizational Affiliation

    ETH Zurich, Institute of Molecular Biology & Biophysics, CH-8093, Zurich, Switzerland. eilika@mol.biol.ethz.ch.



Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChainsSequence LengthOrganismDetailsImage
AAA ATPase forming ring-shaped complexes
A, B, C, D, E, F
A, B, C, D, E, F
609Mycobacterium tuberculosisMutation(s): 0 
Gene Names: 
UniProt
Find proteins for A0A045JPX7 (Mycobacterium tuberculosis)
Explore A0A045JPX7 
Go to UniProtKB:  A0A045JPX7
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA0A045JPX7
Protein Feature View
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  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChainsSequence LengthOrganismDetailsImage
Prokaryotic ubiquitin-like protein PupG66Mycobacterium tuberculosisMutation(s): 0 
Gene Names: 
pupC0094_11500DSI38_15605E5M05_20975E5M52_20890E5M78_20915ERS007661_02567ERS007665_00483ERS007670_00435ERS007679_01034ERS007681_03228ERS007688_03984ERS007720_00611ERS007722_01879ERS007741_02623ERS013471_03479ERS023446_02555ERS024276_00651ERS027646_03180ERS027661_04264ERS094182_01867F6W99_00700FRD82_16980GCL30_10850SAMEA2683035_00453ERS007683_02086ERS013440_03350FPJ30_11495FPJ31_11595FPJ32_11495FPJ33_11535FPJ34_11500FPJ35_11590FPJ36_11490FPJ37_11490FPJ38_11580FPJ39_11500FPJ40_11470FPJ41_11495FPJ42_11390FPJ43_11490FPJ44_11585FPJ45_11500FPJ46_11490FPJ47_11555FPJ48_11505FPJ49_11490FPJ50_11465FPJ51_11460FPJ52_11500FPJ53_11500FPJ54_11505FPJ55_11620FPJ56_11470FPJ57_11480FPJ58_11490FPJ59_11495FPJ60_11495FPJ61_11495FPJ62_11470FPJ63_11525FPJ64_11595FPJ65_11475FPJ66_11495FPJ67_11535FPJ69_11535FPJ70_11535FPJ71_11530FPJ72_10260FPJ73_11480FPJ76_11450FPJ77_11235FPJ78_11500FPJ79_11415FPJ80_11555FPJ81_11640FPJ82_11675FPJ83_10125FPJ84_11440FPJ85_10120FPJ86_10120FPJ87_10115FPJ88_11430FPJ89_11520FPJ90_11450FPJ91_11510FPJ92_11460FPJ93_11445FPJ94_10250FPJ95_11470FPJ96_11600FPJ97_11470FPJ98_11485FPJ99_11485FPK00_11400FPK01_11430FPK02_11495FPK03_11415FPK04_11465FPK05_11505FPK06_11495FPK07_11500FPK08_11570FPK09_11590FPK10_10240FPK11_11510FPK12_11445FPK13_11495FPK14_11500FPK16_11485FPK17_11580FPK18_11545FPK19_11595FPK20_11590FPK21_11480FPK22_11465HRD52_11060HRD53_11040

UniProt
Find proteins for A0A045GWT8 (Mycobacterium tuberculosis)
Explore A0A045GWT8 
Go to UniProtKB:  A0A045GWT8
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA0A045GWT8
Protein Feature View
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Resolution: 4.00 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

Structure Validation

View Full Validation Report




Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
Swiss National Science FoundationSwitzerland--

Revision History  (Full details and data files)

  • Version 1.0: 2022-01-19
    Type: Initial release
  • Version 1.1: 2022-01-26
    Changes: Database references