1g0u: Difference between revisions
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|PDB= 1g0u |SIZE=350|CAPTION= <scene name='initialview01'>1g0u</scene>, resolution 2.40Å | |PDB= 1g0u |SIZE=350|CAPTION= <scene name='initialview01'>1g0u</scene>, resolution 2.40Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM ION'>MG</scene> | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/Proteasome_endopeptidase_complex Proteasome endopeptidase complex], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.25.1 3.4.25.1] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Proteasome_endopeptidase_complex Proteasome endopeptidase complex], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.25.1 3.4.25.1] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1ryp|1RYP]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1g0u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g0u OCA], [http://www.ebi.ac.uk/pdbsum/1g0u PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1g0u RCSB]</span> | |||
}} | }} | ||
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[[Category: Moroder, L.]] | [[Category: Moroder, L.]] | ||
[[Category: Rubin, D M.]] | [[Category: Rubin, D M.]] | ||
[[Category: degradation]] | [[Category: degradation]] | ||
[[Category: ntn-hydrolase]] | [[Category: ntn-hydrolase]] | ||
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[[Category: ubiquitin]] | [[Category: ubiquitin]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:34:09 2008'' | ||
Revision as of 20:34, 30 March 2008
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| , resolution 2.40Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Activity: | Proteasome endopeptidase complex, with EC number 3.4.25.1 | ||||||
| Related: | 1RYP
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
A GATED CHANNEL INTO THE PROTEASOME CORE PARTICLE
OverviewOverview
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.
About this StructureAbout this Structure
1G0U is a Protein complex structure of sequences from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
ReferenceReference
A gated channel into the proteasome core particle., Groll M, Bajorek M, Kohler A, Moroder L, Rubin DM, Huber R, Glickman MH, Finley D, Nat Struct Biol. 2000 Nov;7(11):1062-7. PMID:11062564
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