3wz2: Difference between revisions
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==Crystal structure of Pyrococcus furiosus PbaA, an archaeal homolog of proteasome-assembly chaperone== | ==Crystal structure of Pyrococcus furiosus PbaA, an archaeal homolog of proteasome-assembly chaperone== | ||
<StructureSection load='3wz2' size='340' side='right' caption='[[3wz2]], [[Resolution|resolution]] 2.25Å' scene=''> | <StructureSection load='3wz2' size='340' side='right'caption='[[3wz2]], [[Resolution|resolution]] 2.25Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3wz2]] is a 5 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3wz2]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrfu Pyrfu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WZ2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WZ2 FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3vr0|3vr0]], [[3gaa|3gaa]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3vr0|3vr0]], [[3gaa|3gaa]]</div></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PF0015 ([ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PF0015 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=186497 PYRFU])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3wz2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wz2 OCA], [https://pdbe.org/3wz2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wz2 RCSB], [https://www.ebi.ac.uk/pdbsum/3wz2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wz2 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Pyrfu]] | [[Category: Pyrfu]] | ||
[[Category: Kato, K]] | [[Category: Kato, K]] | ||
Revision as of 08:36, 10 August 2022
Crystal structure of Pyrococcus furiosus PbaA, an archaeal homolog of proteasome-assembly chaperoneCrystal structure of Pyrococcus furiosus PbaA, an archaeal homolog of proteasome-assembly chaperone
Structural highlights
Publication Abstract from PubMedFormation of the eukaryotic proteasome is not a spontaneous process but a highly ordered process assisted by several assembly chaperones. In contrast, archaeal proteasome subunits can spontaneously assemble into an active form. Recent bioinformatic analysis identified the proteasome-assembly chaperone-like proteins, PbaA and PbaB, in archaea. Our previous study showed that the PbaB homotetramer functions as a proteasome activator through its tentacle-like C-terminal segments. However, a functional role of the other homolog PbaA has remained elusive. Here we determined the 2.25-A resolution structure of PbaA, illustrating its disparate tertiary and quaternary structures compared with PbaB. PbaA forms a homopentamer in which the C-terminal segments, with a putative proteasome-activating motif, are packed against the core. These findings offer deeper insights into the molecular evolution relationships between the proteasome-assembly chaperones and the proteasome activators. Crystal structure of archaeal homolog of proteasome-assembly chaperone PbaA.,Sikdar A, Satoh T, Kawasaki M, Kato K Biochem Biophys Res Commun. 2014 Oct 5. pii: S0006-291X(14)01751-3. doi:, 10.1016/j.bbrc.2014.09.114. PMID:25285636[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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