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[[Image:1g0u.jpg|left|200px]]


{{Structure
==A GATED CHANNEL INTO THE PROTEASOME CORE PARTICLE==
|PDB= 1g0u |SIZE=350|CAPTION= <scene name='initialview01'>1g0u</scene>, resolution 2.40&Aring;
<StructureSection load='1g0u' size='340' side='right'caption='[[1g0u]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM ION'>MG</scene>
<table><tr><td colspan='2'>[[1g0u]] is a 20 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G0U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1G0U FirstGlance]. <br>
|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]  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
|GENE=  
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
}}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1g0u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g0u OCA], [https://pdbe.org/1g0u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1g0u RCSB], [https://www.ebi.ac.uk/pdbsum/1g0u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1g0u ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PSA2_YEAST PSA2_YEAST] The proteasome degrades poly-ubiquitinated proteins in the cytoplasm and in the nucleus. It is essential for the regulated turnover of proteins and for the removal of misfolded proteins. The proteasome is a multicatalytic proteinase complex that is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. It has an ATP-dependent proteolytic activity.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g0/1g0u_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1g0u ConSurf].
<div style="clear:both"></div>


'''A GATED CHANNEL INTO THE PROTEASOME CORE PARTICLE'''
==See Also==
 
*[[Proteasome 3D structures|Proteasome 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
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.
[[Category: Large Structures]]
 
==About this Structure==
1G0U is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G0U OCA].
 
==Reference==
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:[http://www.ncbi.nlm.nih.gov/pubmed/11062564 11062564]
[[Category: Proteasome endopeptidase complex]]
[[Category: Protein complex]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Bajorek, M.]]
[[Category: Bajorek M]]
[[Category: Finley, D.]]
[[Category: Finley D]]
[[Category: Glickman, M H.]]
[[Category: Glickman MH]]
[[Category: Groll, M.]]
[[Category: Groll M]]
[[Category: Huber, R.]]
[[Category: Huber R]]
[[Category: Kohler, A.]]
[[Category: Kohler A]]
[[Category: Moroder, L.]]
[[Category: Moroder L]]
[[Category: Rubin, D M.]]
[[Category: Rubin DM]]
[[Category: MG]]
[[Category: degradation]]
[[Category: ntn-hydrolase]]
[[Category: protease]]
[[Category: proteasome]]
[[Category: ubiquitin]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:16:34 2008''

Latest revision as of 10:21, 7 February 2024

A GATED CHANNEL INTO THE PROTEASOME CORE PARTICLEA GATED CHANNEL INTO THE PROTEASOME CORE PARTICLE

Structural highlights

1g0u is a 20 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.4Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PSA2_YEAST The proteasome degrades poly-ubiquitinated proteins in the cytoplasm and in the nucleus. It is essential for the regulated turnover of proteins and for the removal of misfolded proteins. The proteasome is a multicatalytic proteinase complex that is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. It has an ATP-dependent proteolytic activity.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1g0u, resolution 2.40Å

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OCA
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