3c92: Difference between revisions

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<SX load='3c92' size='340' side='right' viewer='molstar' caption='[[3c92]], [[Resolution|resolution]] 6.80&Aring;' scene=''>
<SX load='3c92' size='340' side='right' viewer='molstar' caption='[[3c92]], [[Resolution|resolution]] 6.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3c92]] is a 28 chain structure with sequence from [https://en.wikipedia.org/wiki/"thermoplasma_acidophila"_(sic)_darland_et_al._1970 "thermoplasma acidophila" (sic) darland et al. 1970]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C92 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3C92 FirstGlance]. <br>
<table><tr><td colspan='2'>[[3c92]] is a 28 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermoplasma_acidophilum Thermoplasma acidophilum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C92 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3C92 FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3c91|3c91]]</div></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 6.8&#8491;</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Proteasome_endopeptidase_complex Proteasome endopeptidase complex], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.25.1 3.4.25.1] </span></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=3c92 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c92 OCA], [https://pdbe.org/3c92 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3c92 RCSB], [https://www.ebi.ac.uk/pdbsum/3c92 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3c92 ProSAT]</span></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=3c92 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c92 OCA], [https://pdbe.org/3c92 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3c92 RCSB], [https://www.ebi.ac.uk/pdbsum/3c92 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3c92 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/PSA_THEAC PSA_THEAC]] Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. The T.acidophilum proteasome is able to cleave oligopeptides after Tyr, Leu, Phe, and to a lesser extent after Glu and Arg. Thus, displays chymotrypsin-like activity and low level of caspase-like and trypsin-like activities.<ref>PMID:8999862</ref>  [[https://www.uniprot.org/uniprot/PSB_THEAC PSB_THEAC]] Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. The T.acidophilum proteasome is able to cleave oligopeptides after Tyr, Leu, Phe, and to a lesser extent after Glu and Arg. Thus, displays chymotrypsin-like activity and low level of caspase-like and trypsin-like activities.<ref>PMID:8999862</ref>
[https://www.uniprot.org/uniprot/PSA_THEAC PSA_THEAC] Component of the proteasome core, a large protease complex with broad specificity involved in protein degradation. The T.acidophilum proteasome is able to cleave oligopeptides after Tyr, Leu, Phe, and to a lesser extent after Glu and Arg. Thus, displays chymotrypsin-like activity and low level of caspase-like and trypsin-like activities.<ref>PMID:8999862</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=3c92 ConSurf].
</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=3c92 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Substrates enter the cylindrical 20S proteasome through a gated channel that is regulated by the ATPases in the 19S regulatory particle in eukaryotes or the homologous PAN ATPase complex in archaea. These ATPases contain a conserved C-terminal hydrophobic-tyrosine-X (HbYX) motif that triggers gate opening upon ATP binding. Using cryo-electron microscopy, we identified the sites in the archaeal 20S where PAN's C-terminal residues bind and determined the structures of the gate in its closed and open forms. Peptides containing the HbYX motif bind to 20S in the pockets between neighboring alpha subunits where they interact with conserved residues required for gate opening. This interaction induces a rotation in the alpha subunits and displacement of a reverse-turn loop that stabilizes the open-gate conformation. This mechanism differs from that of PA26/28, which lacks the HbYX motif and does not cause alpha subunit rotation. These findings demonstrated how the ATPases' C termini function to facilitate substrate entry.
Mechanism of gate opening in the 20S proteasome by the proteasomal ATPases.,Rabl J, Smith DM, Yu Y, Chang SC, Goldberg AL, Cheng Y Mol Cell. 2008 May 9;30(3):360-8. PMID:18471981<ref>PMID:18471981</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3c92" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
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</SX>
</SX>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Proteasome endopeptidase complex]]
[[Category: Thermoplasma acidophilum]]
[[Category: Chang, S C]]
[[Category: Chang SC]]
[[Category: Cheng, Y]]
[[Category: Cheng Y]]
[[Category: Goldberg, A L]]
[[Category: Goldberg AL]]
[[Category: Rabl, J]]
[[Category: Rabl J]]
[[Category: Smith, D M]]
[[Category: Smith DM]]
[[Category: Yu, Y]]
[[Category: Yu Y]]
[[Category: Hydrolase]]
[[Category: Protease]]
[[Category: Proteasome]]
[[Category: Protein complex]]
[[Category: Threonine protease]]

Latest revision as of 09:33, 21 February 2024

Thermoplasma acidophilum 20S proteasome with a closed gate

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