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TitleStructural basis of prokaryotic ubiquitin-like protein engagement and translocation by the mycobacterial Mpa-proteasome complex.
Journal, issue, pagesNat Commun, Vol. 13, Issue 1, Page 276, Year 2022
Publish dateJan 12, 2022
AuthorsMikhail Kavalchuk / Ahmad Jomaa / Andreas U Müller / Eilika Weber-Ban /
PubMed AbstractProteasomes are present in eukaryotes, archaea and Actinobacteria, including the human pathogen Mycobacterium tuberculosis, where proteasomal degradation supports persistence inside the host. In ...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.
External linksNat Commun / PubMed:35022401 / PubMed Central
MethodsEM (single particle)
Resolution2.8 - 4.0 Å
Structure data

13694

7px9

EMDB-13694, PDB-7px9:
Substrate-engaged mycobacterial Proteasome-associated ATPase - focused 3D refinement (state A)
Method: EM (single particle) / Resolution: 3.8 Å

13695

7pxa

EMDB-13695, PDB-7pxa:
Open-gate mycobacterium 20S CP proteasome in complex MPA - global 3D refinement
Method: EM (single particle) / Resolution: 2.8 Å

13696

7pxb

EMDB-13696, PDB-7pxb:
Substrate-engaged mycobacterial Proteasome-associated ATPase - focused 3D refinement (state B)
Method: EM (single particle) / Resolution: 4.0 Å

13697

7pxc

EMDB-13697, PDB-7pxc:
Substrate-engaged mycobacterial Proteasome-associated ATPase in complex with open-gate 20S CP - composite map (state A)
Method: EM (single particle) / Resolution: 3.84 Å

13698

7pxd

EMDB-13698, PDB-7pxd:
Substrate-engaged mycobacterial Proteasome-associated ATPase in complex with open-gate 20S CP - composite map (state B)
Method: EM (single particle) / Resolution: 4.0 Å

Chemicals

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM / Adenosine triphosphate

ChemComp-MG:
Unknown entry

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM / Adenosine diphosphate

Source
  • mycobacterium tuberculosis (bacteria)
  • mycobacterium tuberculosis (strain atcc 25618 / h37rv) (bacteria)
KeywordsCYTOSOLIC PROTEIN / AAA motor / ATPAse / mycobacterium / proteasome activator / 20S CP / CHAPERONE

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