PDBsum entry 3h4m

Go to PDB code: 
protein ligands Protein-protein interface(s) links
Hydrolase PDB id
Protein chains
261 a.a. *
ADP ×3
* Residue conservation analysis
PDB id:
Name: Hydrolase
Title: Aaa atpase domain of the proteasome- activating nucleotidase
Structure: Proteasome-activating nucleotidase. Chain: a, b, c. Fragment: pan atpase domain (155-430). Synonym: proteasome regulatory subunit. Engineered: yes
Source: Methanocaldococcus jannaschii. Methanococcus jannaschii. Organism_taxid: 2190. Gene: pan, mj1176. Expressed in: escherichia coli. Expression_system_taxid: 562.
3.11Å     R-factor:   0.223     R-free:   0.277
Authors: P.Jeffrey,F.Zhang,M.Hu,G.Tian,P.Zhang,D.Finley,Y.Shi
Key ref: F.Zhang et al. (2009). Structural insights into the regulatory particle of the proteasome from Methanocaldococcus jannaschii. Mol Cell, 34, 473-484. PubMed id: 19481527
20-Apr-09     Release date:   09-Jun-09    
Go to PROCHECK summary

Protein chains
Pfam   ArchSchema ?
Q58576  (PAN_METJA) -  Proteasome-activating nucleotidase
430 a.a.
261 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   1 term 
  Biological process     protein catabolic process   1 term 
  Biochemical function     hydrolase activity     2 terms  


Mol Cell 34:473-484 (2009)
PubMed id: 19481527  
Structural insights into the regulatory particle of the proteasome from Methanocaldococcus jannaschii.
F.Zhang, M.Hu, G.Tian, P.Zhang, D.Finley, P.D.Jeffrey, Y.Shi.
Eukaryotic proteasome consists of a core particle (CP), which degrades unfolded protein, and a regulatory particle (RP), which is responsible for recognition, ATP-dependent unfolding, and translocation of polyubiquitinated substrate protein. In the archaea Methanocaldococcus jannaschii, the RP is a homohexameric complex of proteasome-activating nucleotidase (PAN). Here, we report the crystal structures of essential elements of the archaeal proteasome: the CP, the ATPase domain of PAN, and a distal subcomplex that is likely the first to encounter substrate. The distal subcomplex contains a coiled-coil segment and an OB-fold domain, both of which appear to be conserved in the eukaryotic proteasome. The OB domains of PAN form a hexameric ring with a 13 A pore, which likely constitutes the outermost constriction of the substrate translocation channel. These studies reveal structural codes and architecture of the complete proteasome, identify potential substrate-binding sites, and uncover unexpected asymmetry in the RP of archaea and eukaryotes.

Literature references that cite this PDB file's key reference

  PubMed id Reference
22237024 G.C.Lander, E.Estrin, M.E.Matyskiela, C.Bashore, E.Nogales, and A.Martin (2012).
Complete subunit architecture of the proteasome regulatory particle.
  Nature, 482, 186-191.  
22183254 J.Maupin-Furlow (2012).
Proteasomes and protein conjugation across domains of life.
  Nat Rev Microbiol, 10, 100-111.  
22037170 G.Tian, S.Park, M.J.Lee, B.Huck, F.McAllister, C.P.Hill, S.P.Gygi, and D.Finley (2011).
An asymmetric interface between the regulatory and core particles of the proteasome.
  Nat Struct Mol Biol, 18, 1259-1267.  
20953180 T.Wang, K.H.Darwin, and H.Li (2010).
Binding-induced folding of prokaryotic ubiquitin-like protein on the Mycobacterium proteasomal ATPase targets substrates for degradation.
  Nat Struct Mol Biol, 17, 1352-1357.
PDB codes: 3m91 3m9b 3m9d 3m9h
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.