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TitleStructural basis for dynamic regulation of the human 26S proteasome.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 113, Issue 46, Page 12991-12996, Year 2016
Publish dateNov 15, 2016
AuthorsShuobing Chen / Jiayi Wu / Ying Lu / Yong-Bei Ma / Byung-Hoon Lee / Zhou Yu / Qi Ouyang / Daniel J Finley / Marc W Kirschner / Youdong Mao /
PubMed AbstractThe proteasome is the major engine of protein degradation in all eukaryotic cells. At the heart of this machine is a heterohexameric ring of AAA (ATPases associated with diverse cellular activities) ...The proteasome is the major engine of protein degradation in all eukaryotic cells. At the heart of this machine is a heterohexameric ring of AAA (ATPases associated with diverse cellular activities) proteins that unfolds ubiquitylated target proteins that are concurrently translocated into a proteolytic chamber and degraded into peptides. Using cryoelectron microscopy, we determined a near-atomic-resolution structure of the 2.5-MDa human proteasome in its ground state, as well as subnanometer-resolution structures of the holoenzyme in three alternative conformational states. The substrate-unfolding AAA-ATPase channel is narrowed by 10 inward-facing pore loops arranged into two helices that run in parallel with each other, one hydrophobic in character and the other highly charged. The gate of the core particle was unexpectedly found closed in the ground state and open in only one of the alternative states. Coordinated, stepwise conformational changes of the regulatory particle couple ATP hydrolysis to substrate translocation and regulate gating of the core particle, leading to processive degradation.
External linksProc Natl Acad Sci U S A / PubMed:27791164 / PubMed Central
MethodsEM (single particle)
Resolution3.8 - 8.0 Å
Structure data

8332

5t0c

EMDB-8332, PDB-5t0c:
Structural basis for dynamic regulation of the human 26S proteasome
Method: EM (single particle) / Resolution: 3.8 Å

8333

5t0c

EMDB-8333, PDB-5t0c:
Structural basis for dynamic regulation of the human 26S proteasome
Method: EM (single particle) / Resolution: 3.8 Å

8334

5t0g

EMDB-8334, PDB-5t0g:
Structural basis for dynamic regulation of the human 26S proteasome
Method: EM (single particle) / Resolution: 4.4 Å

8335

5t0h

EMDB-8335, PDB-5t0h:
Structural basis for dynamic regulation of the human 26S proteasome
Method: EM (single particle) / Resolution: 6.8 Å

8336

5t0i

EMDB-8336, PDB-5t0i:
Structural basis for dynamic regulation of the human 26S proteasome
Method: EM (single particle) / Resolution: 8.0 Å

8337

5t0j

EMDB-8337, PDB-5t0j:
Structural basis for dynamic regulation of the human 26S proteasome
Method: EM (single particle) / Resolution: 8.0 Å

Chemicals

ChemComp-ZN:
Unknown entry

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

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

Source
  • homo sapiens (human)
KeywordsHYDROLASE / ubiquitin-proteasome system / AAA-ATPase

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