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| | <StructureSection load='6jpt' size='340' side='right'caption='[[6jpt]], [[Resolution|resolution]] 0.96Å' scene=''> | | <StructureSection load='6jpt' size='340' side='right'caption='[[6jpt]], [[Resolution|resolution]] 0.96Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6jpt]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JPT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6JPT FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6jpt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JPT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6JPT FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=SCN:THIOCYANATE+ION'>SCN</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 0.96Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2z5e|2z5e]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=SCN:THIOCYANATE+ION'>SCN</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6jpt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jpt OCA], [http://pdbe.org/6jpt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6jpt RCSB], [http://www.ebi.ac.uk/pdbsum/6jpt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6jpt 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=6jpt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jpt OCA], [https://pdbe.org/6jpt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6jpt RCSB], [https://www.ebi.ac.uk/pdbsum/6jpt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6jpt ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PSMG3_HUMAN PSMG3_HUMAN]] Chaperone protein which promotes assembly of the 20S proteasome. May cooperate with PSMG1-PSMG2 heterodimers to orchestrate the correct assembly of proteasomes.<ref>PMID:17189198</ref> | + | [https://www.uniprot.org/uniprot/PSMG3_HUMAN PSMG3_HUMAN] Chaperone protein which promotes assembly of the 20S proteasome. May cooperate with PSMG1-PSMG2 heterodimers to orchestrate the correct assembly of proteasomes.<ref>PMID:17189198</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Kato, K]] | + | [[Category: Kato K]] |
| - | [[Category: Kurimoto, E]] | + | [[Category: Kurimoto E]] |
| - | [[Category: Okamoto, K]] | + | [[Category: Okamoto K]] |
| - | [[Category: Satoh, T]] | + | [[Category: Satoh T]] |
| - | [[Category: Tanaka, K]] | + | [[Category: Tanaka K]] |
| - | [[Category: Yagi-Utsumi, M]] | + | [[Category: Yagi-Utsumi M]] |
| - | [[Category: Chaperone]]
| + | |
| - | [[Category: Proteasome assembly chaperone]]
| + | |
| Structural highlights
Function
PSMG3_HUMAN Chaperone protein which promotes assembly of the 20S proteasome. May cooperate with PSMG1-PSMG2 heterodimers to orchestrate the correct assembly of proteasomes.[1]
Publication Abstract from PubMed
The 26S proteasome is critical for the selective degradation of proteins in eukaryotic cells. This enzyme complex is composed of approximately 70 subunits, including the structurally homologous proteins alpha1-alpha7, which combine to form heptameric rings. The correct arrangement of these alpha subunits is essential for the function of the proteasome, but their assembly does not occur autonomously. Assembly of the alpha subunit is assisted by several chaperones, including the PAC3-PAC4 heterodimer. In this study we showed that the PAC3-PAC4 heterodimer functions as a molecular matchmaker, stabilizing the alpha4-alpha5-alpha6 subcomplex during the assembly of the alpha-ring. We solved a 0.96-A atomic resolution crystal structure for a PAC3 homodimer which, in conjunction with nuclear magnetic resonance (NMR) data, highlighted the mobility of the loop comprised of residues 51 to 61. Based on these structural and dynamic data, we created a three-dimensional model of the PAC3-4/alpha4/alpha5/alpha6 quintet complex, and used this model to investigate the molecular and structural basis of the mechanism of proteasome alpha subunit assembly, as mediated by the PAC3-PAC4 heterodimeric chaperone. Our results provide a potential basis for the development of selective inhibitors against proteasome biogenesis.
Molecular and Structural Basis of the Proteasome alpha Subunit Assembly Mechanism Mediated by the Proteasome-Assembling Chaperone PAC3-PAC4 Heterodimer.,Satoh T, Yagi-Utsumi M, Okamoto K, Kurimoto E, Tanaka K, Kato K Int J Mol Sci. 2019 May 7;20(9). pii: ijms20092231. doi: 10.3390/ijms20092231. PMID:31067643[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hirano Y, Hayashi H, Iemura S, Hendil KB, Niwa S, Kishimoto T, Kasahara M, Natsume T, Tanaka K, Murata S. Cooperation of multiple chaperones required for the assembly of mammalian 20S proteasomes. Mol Cell. 2006 Dec 28;24(6):977-84. PMID:17189198 doi:http://dx.doi.org/10.1016/j.molcel.2006.11.015
- ↑ Satoh T, Yagi-Utsumi M, Okamoto K, Kurimoto E, Tanaka K, Kato K. Molecular and Structural Basis of the Proteasome alpha Subunit Assembly Mechanism Mediated by the Proteasome-Assembling Chaperone PAC3-PAC4 Heterodimer. Int J Mol Sci. 2019 May 7;20(9). pii: ijms20092231. doi: 10.3390/ijms20092231. PMID:31067643 doi:http://dx.doi.org/10.3390/ijms20092231
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