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PDBsum entry 1vsy

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protein Protein-protein interface(s) links
Hydrolase PDB id
1vsy
Jmol
Contents
Protein chains
243 a.a. *
231 a.a. *
232 a.a. *
227 a.a. *
250 a.a. *
234 a.a. *
244 a.a. *
196 a.a. *
222 a.a. *
204 a.a. *
198 a.a. *
212 a.a. *
222 a.a. *
233 a.a. *
76 a.a. *
799 a.a. *
997 a.a. *
* Residue conservation analysis
PDB id:
1vsy
Name: Hydrolase
Title: Proteasome activator complex
Structure: Proteasome component c7-alpha. Chain: a, o. Synonym: macropain subunit c7-alpha, proteinase ysce subuni multicatalytic endopeptidase complex c7, proteasome compone scl1 suppressor protein. Proteasome component y7. Chain: b, p. Synonym: macropain subunit y7, proteinase ysce subunit 7, multicatalytic endopeptidase complex subunit y7.
Source: Saccharomyces cerevisiae. Organism_taxid: 4932. Organism_taxid: 4932
Resolution:
3.00Å     R-factor:   0.196     R-free:   0.250
Authors: C.P.Hill,F.G.Whitby
Key ref: K.Sadre-Bazzaz et al. (2010). Structure of a Blm10 complex reveals common mechanisms for proteasome binding and gate opening. Mol Cell, 37, 728-735. PubMed id: 20227375
Date:
05-Jan-10     Release date:   16-Jun-10    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P21243  (PSA6_YEAST) -  Proteasome subunit alpha type-1
Seq:
Struc:
252 a.a.
243 a.a.
Protein chains
Pfam   ArchSchema ?
P23639  (PSA2_YEAST) -  Proteasome subunit alpha type-2
Seq:
Struc:
250 a.a.
231 a.a.
Protein chains
Pfam   ArchSchema ?
P23638  (PSA4_YEAST) -  Proteasome subunit alpha type-3
Seq:
Struc:
258 a.a.
232 a.a.
Protein chains
Pfam   ArchSchema ?
P40303  (PSA7_YEAST) -  Proteasome subunit alpha type-4
Seq:
Struc:
254 a.a.
227 a.a.
Protein chains
Pfam   ArchSchema ?
P32379  (PSA5_YEAST) -  Proteasome subunit alpha type-5
Seq:
Struc:
260 a.a.
250 a.a.
Protein chains
Pfam   ArchSchema ?
P40302  (PSA1_YEAST) -  Proteasome subunit alpha type-6
Seq:
Struc:
234 a.a.
234 a.a.
Protein chains
Pfam   ArchSchema ?
P21242  (PSA3_YEAST) -  Probable proteasome subunit alpha type-7
Seq:
Struc:
288 a.a.
244 a.a.
Protein chains
Pfam   ArchSchema ?
P38624  (PSB6_YEAST) -  Proteasome subunit beta type-1
Seq:
Struc:
215 a.a.
196 a.a.*
Protein chains
Pfam   ArchSchema ?
P25043  (PSB7_YEAST) -  Proteasome subunit beta type-2
Seq:
Struc:
261 a.a.
222 a.a.
Protein chains
Pfam   ArchSchema ?
P25451  (PSB3_YEAST) -  Proteasome subunit beta type-3
Seq:
Struc:
205 a.a.
204 a.a.
Protein chains
Pfam   ArchSchema ?
P22141  (PSB2_YEAST) -  Proteasome subunit beta type-4
Seq:
Struc:
198 a.a.
198 a.a.
Protein chains
Pfam   ArchSchema ?
P30656  (PSB5_YEAST) -  Proteasome subunit beta type-5
Seq:
Struc:
287 a.a.
212 a.a.*
Protein chains
Pfam   ArchSchema ?
P23724  (PSB1_YEAST) -  Proteasome subunit beta type-6
Seq:
Struc:
241 a.a.
222 a.a.
Protein chains
Pfam   ArchSchema ?
P30657  (PSB4_YEAST) -  Proteasome subunit beta type-7
Seq:
Struc:
266 a.a.
233 a.a.
Protein chains
Pfam   ArchSchema ?
P43583  (BLM10_YEAST) -  Proteasome activator BLM10
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
2143 a.a.
76 a.a.
Protein chains
Pfam   ArchSchema ?
P43583  (BLM10_YEAST) -  Proteasome activator BLM10
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
2143 a.a.
799 a.a.*
Protein chains
Pfam   ArchSchema ?
P43583  (BLM10_YEAST) -  Proteasome activator BLM10
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
2143 a.a.
997 a.a.*
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 9 residue positions (black crosses)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     nuclear outer membrane-endoplasmic reticulum membrane network   9 terms 
  Biological process     proteolysis   7 terms 
  Biochemical function     molecular_function     7 terms  

 

 
Mol Cell 37:728-735 (2010)
PubMed id: 20227375  
 
 
Structure of a Blm10 complex reveals common mechanisms for proteasome binding and gate opening.
K.Sadre-Bazzaz, F.G.Whitby, H.Robinson, T.Formosa, C.P.Hill.
 
  ABSTRACT  
 
The proteasome is an abundant protease that is critically important for numerous cellular pathways. Proteasomes are activated in vitro by three known classes of proteins/complexes, including Blm10/PA200. Here, we report a 3.4 A resolution crystal structure of a proteasome-Blm10 complex, which reveals that Blm10 surrounds the proteasome entry pore in the 1.2 MDa complex to form a largely closed dome that is expected to restrict access of potential substrates. This architecture and the observation that Blm10 induces a disordered proteasome gate structure challenge the assumption that Blm10 functions as an activator of proteolysis in vivo. The Blm10 C terminus binds in the same manner as seen for 11S activators and inferred for 19S/PAN activators and indicates a unified model for gate opening. We also demonstrate that Blm10 acts to maintain mitochondrial function. Consistent with the structural data, the C-terminal residues of Blm10 are needed for this activity.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
22119785 J.C.Christianson, J.A.Olzmann, T.A.Shaler, M.E.Sowa, E.J.Bennett, C.M.Richter, R.E.Tyler, E.J.Greenblatt, J.W.Harper, and R.R.Kopito (2012).
Defining human ERAD networks through an integrative mapping strategy.
  Nat Cell Biol, 14, 93.  
20427185 L.Bedford, S.Paine, P.W.Sheppard, R.J.Mayer, and J.Roelofs (2010).
Assembly, structure, and function of the 26S proteasome.
  Trends Cell Biol, 20, 391-401.  
20930034 Y.Xie (2010).
Structure, assembly and homeostatic regulation of the 26S proteasome.
  J Mol Cell Biol, 2, 308-317.  
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.