1G0U

A GATED CHANNEL INTO THE PROTEASOME CORE PARTICLE


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.40 Å
  • R-Value Free: 0.303 
  • R-Value Work: 0.250 
  • R-Value Observed: 0.260 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

A gated channel into the proteasome core particle.

Groll, M.Bajorek, M.Kohler, A.Moroder, L.Rubin, D.M.Huber, R.Glickman, M.H.Finley, D.

(2000) Nat Struct Biol 7: 1062-1067

  • DOI: https://doi.org/10.1038/80992
  • Primary Citation of Related Structures:  
    1G0U

  • PubMed Abstract: 

    The core particle (CP) of the yeast proteasome is composed of four heptameric rings of subunits arranged in a hollow, barrel-like structure. We report that the CP is autoinhibited by the N-terminal tails of the outer (alpha) ring subunits. Crystallographic analysis showed that deletion of the tail of the alpha 3-subunit opens a channel into the proteolytically active interior chamber of the CP, thus derepressing peptide hydrolysis. In the latent state of the particle, the tails prevent substrate entry by imposing topological closure on the CP. Inhibition by the alpha-subunit tails is relieved upon binding of the regulatory particle to the CP to form the proteasome holoenzyme.


  • Organizational Affiliation

    Max-Planck-Institut für Biochemie, D-82152 Martinsried, Germany. [email protected]


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
PROTEASOME COMPONENT Y7
A, O
250Saccharomyces cerevisiaeMutation(s): 0 
EC: 3.4.99.46
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
PROTEASOME COMPONENT Y13
B, P
245Saccharomyces cerevisiaeMutation(s): 0 
EC: 3.4.99.46
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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
PROTEASOME COMPONENT PRE6
C, Q
243Saccharomyces cerevisiaeMutation(s): 0 
EC: 3.4.99.46
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Entity ID: 4
MoleculeChains Sequence LengthOrganismDetailsImage
PROTEASOME COMPONENT PUP2
D, R
241Saccharomyces cerevisiaeMutation(s): 0 
EC: 3.4.99.46
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Entity ID: 5
MoleculeChains Sequence LengthOrganismDetailsImage
PROTEASOME COMPONENT PRE5
E, S
234Saccharomyces cerevisiaeMutation(s): 0 
EC: 3.4.99.46
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Entity ID: 6
MoleculeChains Sequence LengthOrganismDetailsImage
PROTEASOME COMPONENT C1
F, T
248Saccharomyces cerevisiaeMutation(s): 0 
EC: 3.4.99.46
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Entity ID: 7
MoleculeChains Sequence LengthOrganismDetailsImage
PROTEASOME COMPONENT C7-ALPHA
G, U
252Saccharomyces cerevisiaeMutation(s): 0 
EC: 3.4.99.46
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Entity ID: 8
MoleculeChains Sequence LengthOrganismDetailsImage
PROTEASOME COMPONENT PUP1
H, V
222Saccharomyces cerevisiaeMutation(s): 0 
EC: 3.4.99.46 (PDB Primary Data), 3.4.25.1 (UniProt)
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Entity ID: 9
MoleculeChains Sequence LengthOrganismDetailsImage
PROTEASOME COMPONENT PUP3
I, W
205Saccharomyces cerevisiaeMutation(s): 0 
EC: 3.4.99.46
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Entity ID: 10
MoleculeChains Sequence LengthOrganismDetailsImage
PROTEASOME COMPONENT C11
J, X
198Saccharomyces cerevisiaeMutation(s): 0 
EC: 3.4.99.46
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Entity ID: 11
MoleculeChains Sequence LengthOrganismDetailsImage
PROTEASOME COMPONENT PRE2
K, Y
212Saccharomyces cerevisiaeMutation(s): 0 
EC: 3.4.99.46 (PDB Primary Data), 3.4.25.1 (UniProt)
UniProt
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Entity ID: 12
MoleculeChains Sequence LengthOrganismDetailsImage
PROTEASOME COMPONENT C5
L, Z
241Saccharomyces cerevisiaeMutation(s): 0 
EC: 3.4.99.46
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Entity ID: 13
MoleculeChains Sequence LengthOrganismDetailsImage
PROTEASOME COMPONENT PRE4AA [auth 1],
M
266Saccharomyces cerevisiaeMutation(s): 0 
EC: 3.4.99.46
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Entity ID: 14
MoleculeChains Sequence LengthOrganismDetailsImage
PROTEASOME COMPONENT PRE3BA [auth 2],
N
196Saccharomyces cerevisiaeMutation(s): 0 
EC: 3.4.99.46 (PDB Primary Data), 3.4.25.1 (UniProt)
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Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
MG
Query on MG

Download Ideal Coordinates CCD File 
CA [auth F]
DA [auth G]
EA [auth G]
FA [auth H]
GA [auth I]
CA [auth F],
DA [auth G],
EA [auth G],
FA [auth H],
GA [auth I],
HA [auth I],
IA [auth K],
JA [auth L],
KA [auth L],
LA [auth N],
MA [auth T],
NA [auth U],
OA [auth U],
PA [auth V],
QA [auth W],
RA [auth W],
SA [auth Y],
TA [auth Z],
UA [auth Z],
VA [auth 2]
MAGNESIUM ION
Mg
JLVVSXFLKOJNIY-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.40 Å
  • R-Value Free: 0.303 
  • R-Value Work: 0.250 
  • R-Value Observed: 0.260 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 135.18α = 90
b = 301.1β = 113
c = 144.1γ = 90
Software Package:
Software NamePurpose
DENZOdata reduction
SCALEPACKdata scaling
X-PLORmodel building
X-PLORrefinement
X-PLORphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2000-11-06
    Type: Initial release
  • Version 1.1: 2008-04-27
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2024-02-07
    Changes: Data collection, Database references, Derived calculations