5wtq: Difference between revisions

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'''Unreleased structure'''


The entry 5wtq is ON HOLD  until Paper Publication
==Crystal structure of human proteasome-assembling chaperone PAC4==
<StructureSection load='5wtq' size='340' side='right' caption='[[5wtq]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5wtq]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WTQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5WTQ FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</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=5wtq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wtq OCA], [http://pdbe.org/5wtq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wtq RCSB], [http://www.ebi.ac.uk/pdbsum/5wtq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wtq ProSAT]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/PSMG4_HUMAN PSMG4_HUMAN]] Chaperone protein which promotes assembly of the 20S proteasome.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The 26S proteasome is a large protein complex, responsible for degradation of ubiquinated proteins in eukaryotic cells. Eukaryotic proteasome formation is a highly ordered process that is assisted by several assembly chaperones. The assembly of its catalytic 20S core particle depends on at least five proteasome-specific chaperones, i.e., proteasome-assembling chaperons 1-4 (PAC1-4) and proteasome maturation protein (POMP). The orthologues of yeast assembly chaperones have been structurally characterized, whereas most mammalian assembly chaperones are not. In the present study, we determined a crystal structure of human PAC4 at 1.90-A resolution. Our crystallographic data identify a hydrophobic surface that is surrounded by charged residues. The hydrophobic surface is complementary to that of its binding partner, PAC3. The surface also exhibits charge complementarity with the proteasomal alpha4-5 subunits. This will provide insights into human proteasome-assembling chaperones as potential anticancer drug targets.


Authors: Kurimoto, E., Satoh, T., Ito, Y., Ishihara, E., Tanaka, K., Kato, K.
Crystal structure of human proteasome assembly chaperone PAC4 involved in proteasome formation.,Kurimoto E, Satoh T, Ito Y, Ishihara E, Okamoto K, Yagi-Utsumi M, Tanaka K, Kato K Protein Sci. 2017 May;26(5):1080-1085. doi: 10.1002/pro.3153. Epub 2017 Mar 16. PMID:28263418<ref>PMID:28263418</ref>


Description: Crystal structure of human proteasome assembly chaperone PAC4
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 5wtq" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Ishihara, E]]
[[Category: Ito, Y]]
[[Category: Kato, K]]
[[Category: Kurimoto, E]]
[[Category: Satoh, T]]
[[Category: Satoh, T]]
[[Category: Kurimoto, E]]
[[Category: Kato, K]]
[[Category: Tanaka, K]]
[[Category: Tanaka, K]]
[[Category: Ishihara, E]]
[[Category: Chaperone]]
[[Category: Ito, Y]]
[[Category: Proteasome assembly chaperone]]
[[Category: Transferase]]
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