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PDBsum entry 3ipm
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protein Protein-protein interface(s) links
Hydrolase/hydrolase activator PDB id
3ipm

 

 

 

 

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Contents
Protein chains
(+ 1 more) 227 a.a. *
(+ 1 more) 203 a.a. *
(+ 1 more) 219 a.a. *
* Residue conservation analysis
PDB id:
3ipm
Name: Hydrolase/hydrolase activator
Title: Crystal structure of archaeal 20s proteasome in complex with thE C- terminus of pan
Structure: Proteasome subunit alpha. Chain: a, b, c, d, e, f, g. Synonym: 20s proteasome alpha subunit,proteasome core protein psma. Engineered: yes. Proteasome subunit beta. Chain: h, i, j, k, l, m, n. Synonym: 20s proteasome beta subunit,proteasome core protein psmb. Engineered: yes. Proteasome activator pa26, proteasome-activating
Source: Thermoplasma acidophilum. Organism_taxid: 2303. Gene: psma, ta1288. Expressed in: escherichia coli. Expression_system_taxid: 469008. Gene: psmb, ta0612. Trypanosoma brucei brucei, methanocaldococcus jannaschii. Organism_taxid: 5691, 2190.
Resolution:
4.00Å     R-factor:   0.249     R-free:   0.284
Authors: Y.Yu,Y.Cheng
Key ref: Y.Yu et al. (2010). Interactions of PAN's C-termini with archaeal 20S proteasome and implications for the eukaryotic proteasome-ATPase interactions. Embo J, 29, 692-702. PubMed id: 20019667
Date:
17-Aug-09     Release date:   29-Dec-09    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P25156  (PSA_THEAC) -  Proteasome subunit alpha from Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Seq:
Struc: 		233 a.a.
227 a.a.
Protein chains
Pfam   ArchSchema ?
P28061  (PSB_THEAC) -  Proteasome subunit beta from Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Seq:
Struc: 		211 a.a.
203 a.a.
Protein chains
Pfam   ArchSchema ?
Q38BM8  (Q38BM8_TRYB2) -  Proteasome activator protein PA26 from Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Seq:
Struc: 		231 a.a.
219 a.a.*
Protein chains
Pfam   ArchSchema ?
Q58576  (PAN_METJA) -  Proteasome-activating nucleotidase from Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Seq:
Struc: 		430 a.a.
219 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 197 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class 1: Chains A, B, C, D, E, F, G, H, I, J, K, L, M, N: E.C.3.4.25.1  - proteasome endopeptidase complex.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Cleavage at peptide bonds with very broad specificity.
   Enzyme class 2: Chains O, P, Q, R, S, T, U: E.C.?
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

 

 
Embo J 29:692-702 (2010)
PubMed id: 20019667  
 
 
Interactions of PAN's C-termini with archaeal 20S proteasome and implications for the eukaryotic proteasome-ATPase interactions.
Y.Yu, D.M.Smith, H.M.Kim, V.Rodriguez, A.L.Goldberg, Y.Cheng.
 
  ABSTRACT  
 
Protein degradation in the 20S proteasome is regulated in eukaryotes by the 19S ATPase complex and in archaea by the homologous PAN ATPase ring complex. Subunits of these hexameric ATPases contain on their C-termini a conserved hydrophobic-tyrosine-X (HbYX) motif that docks into pockets in the 20S to stimulate the opening of a gated substrate entry channel. Here, we report the crystal structure of the archaeal 20S proteasome in complex with the C-terminus of the archaeal proteasome regulatory ATPase, PAN. This structure defines the detailed interactions between the critical C-terminal HbYX motif and the 20S alpha-subunits and indicates that the intersubunit pocket in the 20S undergoes an induced-fit conformational change on binding of the HbYX motif. This structure together with related mutagenesis data suggest how in eukaryotes certain proteasomal ATPases bind to specific pockets in an asymmetrical manner to regulate gate opening.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
22183254 J.Maupin-Furlow (2012).
Proteasomes and protein conjugation across domains of life.
  Nat Rev Microbiol, 10, 100-111.  
21335235 D.M.Smith, H.Fraga, C.Reis, G.Kafri, and A.L.Goldberg (2011).
ATP binds to proteasomal ATPases in pairs with distinct functional effects, implying an ordered reaction cycle.
  Cell, 144, 526-538.  
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.  
20203624 F.Striebel, M.Hunkeler, H.Summer, and E.Weber-Ban (2010).
The mycobacterial Mpa-proteasome unfolds and degrades pupylated substrates by engaging Pup's N-terminus.
  EMBO J, 29, 1262-1271.  
20541423 N.Gallastegui, and M.Groll (2010).
The 26S proteasome: assembly and function of a destructive machine.
  Trends Biochem Sci, 35, 634-642.  
21098295 S.Bohn, F.Beck, E.Sakata, T.Walzthoeni, M.Beck, R.Aebersold, F.Förster, W.Baumeister, and S.Nickell (2010).
Structure of the 26S proteasome from Schizosaccharomyces pombe at subnanometer resolution.
  Proc Natl Acad Sci U S A, 107, 20992-20997.  
20360109 T.L.Religa, R.Sprangers, and L.E.Kay (2010).
Dynamic regulation of archaeal proteasome gate opening as studied by TROSY NMR.
  Science, 328, 98.
PDB codes: 2ku1 2ku2
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.

 

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