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PDBsum entry 1vsy
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Contents |
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243 a.a.
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231 a.a.
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232 a.a.
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227 a.a.
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250 a.a.
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234 a.a.
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244 a.a.
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196 a.a.
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222 a.a.
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204 a.a.
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198 a.a.
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212 a.a.
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222 a.a.
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233 a.a.
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76 a.a.
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799 a.a.
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997 a.a.
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* Residue conservation analysis
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Obsolete entry |
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PDB id:
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| Name: |
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Hydrolase
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Title:
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Proteasome activator complex
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Structure:
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Proteasome component c7-alpha. Chain: a, o. Synonym: macropain subunit c7-alpha, proteinase ysce subunit 7, multicatalytic endopeptidase complex c7, proteasome component y8, scl1 suppressor protein. Proteasome component y7. Chain: b, p. Synonym: macropain subunit y7, proteinase ysce subunit 7, multicatalytic endopeptidase complex subunit y7.
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Source:
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Saccharomyces cerevisiae. Organism_taxid: 4932. Organism_taxid: 4932
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Resolution:
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3.00Å
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R-factor:
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0.196
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R-free:
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0.250
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Authors:
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C.P.Hill,F.G.Whitby
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Key ref:
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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:
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Date:
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05-Jan-10
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Release date:
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16-Jun-10
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PROCHECK
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Headers
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References
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P21243
(PSA1_YEAST) -
Proteasome subunit alpha type-1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
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Seq:
Struc:
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252 a.a.
243 a.a.
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P23639
(PSA2_YEAST) -
Proteasome subunit alpha type-2 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
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Seq:
Struc:
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250 a.a.
231 a.a.
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P23638
(PSA3_YEAST) -
Proteasome subunit alpha type-3 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
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Seq:
Struc:
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258 a.a.
232 a.a.
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P40303
(PSA4_YEAST) -
Proteasome subunit alpha type-4 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
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Seq:
Struc:
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254 a.a.
227 a.a.
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P32379
(PSA5_YEAST) -
Proteasome subunit alpha type-5 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
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Seq:
Struc:
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260 a.a.
250 a.a.
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P40302
(PSA6_YEAST) -
Proteasome subunit alpha type-6 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
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Seq:
Struc:
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234 a.a.
234 a.a.
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P21242
(PSA7_YEAST) -
Probable proteasome subunit alpha type-7 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
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Seq:
Struc:
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288 a.a.
244 a.a.
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P38624
(PSB1_YEAST) -
Proteasome subunit beta type-1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
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Seq:
Struc:
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215 a.a.
196 a.a.*
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P25043
(PSB2_YEAST) -
Proteasome subunit beta type-2 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
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Seq:
Struc:
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261 a.a.
222 a.a.
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P25451
(PSB3_YEAST) -
Proteasome subunit beta type-3 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
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Seq:
Struc:
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205 a.a.
204 a.a.
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P22141
(PSB4_YEAST) -
Proteasome subunit beta type-4 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
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Seq:
Struc:
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198 a.a.
198 a.a.
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P30656
(PSB5_YEAST) -
Proteasome subunit beta type-5 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
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Seq:
Struc:
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287 a.a.
212 a.a.*
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P23724
(PSB6_YEAST) -
Proteasome subunit beta type-6 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
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Seq:
Struc:
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241 a.a.
222 a.a.
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P30657
(PSB7_YEAST) -
Proteasome subunit beta type-7 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
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Seq:
Struc:
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266 a.a.
233 a.a.
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P43583
(BLM10_YEAST) -
Proteasome activator BLM10 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
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Seq:
Struc:
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2143 a.a.
76 a.a.
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Mol Cell
37:728-735
(2010)
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PubMed id:
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Structure of a Blm10 complex reveals common mechanisms for proteasome binding and gate opening.
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K.Sadre-Bazzaz,
F.G.Whitby,
H.Robinson,
T.Formosa,
C.P.Hill.
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ABSTRACT
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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.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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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.
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Nat Cell Biol,
14,
93.
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L.Bedford,
S.Paine,
P.W.Sheppard,
R.J.Mayer,
and
J.Roelofs
(2010).
Assembly, structure, and function of the 26S proteasome.
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Trends Cell Biol,
20,
391-401.
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Y.Xie
(2010).
Structure, assembly and homeostatic regulation of the 26S proteasome.
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J Mol Cell Biol,
2,
308-317.
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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.
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Links
