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(+ 8 more)
232 a.a.
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(+ 8 more)
202 a.a.
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* Residue conservation analysis
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PDB id:
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Hydrolase
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Title:
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Proteasome 20s core particle from methanocaldococcus jannaschii
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Structure:
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Proteasome subunit alpha. Chain: a, b, c, d, e, f, g, h, i, j, k, l, m, n. Synonym: multicatalytic endopeptidase complex subunit alpha, 20s proteasome subunit alpha. Engineered: yes. Proteasome subunit beta. Chain: a, b, c, d, e, f, g, h, i, j, k, l, m, n. Synonym: multicatalytic endopeptidase complex subunit beta. Engineered: yes
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Source:
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Methanocaldococcus jannaschii. Methanococcus jannaschii. Organism_taxid: 2190. Gene: psma, mj0591. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: psmb, mj1237. Expression_system_taxid: 562
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Resolution:
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4.10Å
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R-factor:
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0.257
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R-free:
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0.325
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Authors:
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P.D.Jeffrey,F.Zhang,M.Hu,G.Tian,P.Zhang,D.Finley,Y.Shi
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Key ref:
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F.Zhang
et al.
(2009).
Structural insights into the regulatory particle of the proteasome from Methanocaldococcus jannaschii.
Mol Cell,
34,
473-484.
PubMed id:
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Date:
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20-Apr-09
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Release date:
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09-Jun-09
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PROCHECK
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Headers
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References
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Enzyme class:
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Chains A, B, C, D, E, F, G, a, b, c, d, e, f, g, H, I, J, K, L, M, N, h, i, j, k, l, m, n:
E.C.3.4.25.1
- proteasome endopeptidase complex.
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Reaction:
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Cleavage at peptide bonds with very broad specificity.
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Mol Cell
34:473-484
(2009)
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PubMed id:
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Structural insights into the regulatory particle of the proteasome from Methanocaldococcus jannaschii.
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F.Zhang,
M.Hu,
G.Tian,
P.Zhang,
D.Finley,
P.D.Jeffrey,
Y.Shi.
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ABSTRACT
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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.
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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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G.C.Lander,
E.Estrin,
M.E.Matyskiela,
C.Bashore,
E.Nogales,
and
A.Martin
(2012).
Complete subunit architecture of the proteasome regulatory particle.
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Nature,
482,
186-191.
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J.Maupin-Furlow
(2012).
Proteasomes and protein conjugation across domains of life.
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Nat Rev Microbiol,
10,
100-111.
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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.
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Nat Struct Mol Biol,
18,
1259-1267.
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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.
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Nat Struct Mol Biol,
17,
1352-1357.
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PDB codes:
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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.
Where a reference describes a PDB structure, the PDB
codes are
shown on the right.
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Links
