4v7o
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4v7o]] is a 40 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1vsy 1vsy] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3l5q 3l5q]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V7O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4V7O FirstGlance]. <br> | <table><tr><td colspan='2'>[[4v7o]] is a 40 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1vsy 1vsy] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3l5q 3l5q]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V7O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4V7O FirstGlance]. <br> | ||
| - | </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=4v7o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v7o OCA], [https://pdbe.org/4v7o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4v7o RCSB], [https://www.ebi.ac.uk/pdbsum/4v7o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4v7o ProSAT]</span></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]] 3.005Å</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=4v7o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v7o OCA], [https://pdbe.org/4v7o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4v7o RCSB], [https://www.ebi.ac.uk/pdbsum/4v7o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4v7o ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/PSB6_YEAST PSB6_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. | [https://www.uniprot.org/uniprot/PSB6_YEAST PSB6_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. | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The proteasome is an abundant protease that is critically important for numerous cellular pathways. Proteasomes are activated in vitro by three known classes of proteins/complexes, including Blm10/PA200. Here, we report a 3.4 A resolution crystal structure of a proteasome-Blm10 complex, which reveals that Blm10 surrounds the proteasome entry pore in the 1.2 MDa complex to form a largely closed dome that is expected to restrict access of potential substrates. This architecture and the observation that Blm10 induces a disordered proteasome gate structure challenge the assumption that Blm10 functions as an activator of proteolysis in vivo. The Blm10 C terminus binds in the same manner as seen for 11S activators and inferred for 19S/PAN activators and indicates a unified model for gate opening. We also demonstrate that Blm10 acts to maintain mitochondrial function. Consistent with the structural data, the C-terminal residues of Blm10 are needed for this activity. | ||
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| - | Structure of a Blm10 complex reveals common mechanisms for proteasome binding and gate opening.,Sadre-Bazzaz K, Whitby FG, Robinson H, Formosa T, Hill CP Mol Cell. 2010 Mar 12;37(5):728-35. PMID:20227375<ref>PMID:20227375</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 4v7o" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Proteasome 3D structures|Proteasome 3D structures]] | *[[Proteasome 3D structures|Proteasome 3D structures]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
Proteasome Activator Complex
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