3wz2: Difference between revisions
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<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=3wz2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wz2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3wz2 RCSB], [http://www.ebi.ac.uk/pdbsum/3wz2 PDBsum]</span></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=3wz2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wz2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3wz2 RCSB], [http://www.ebi.ac.uk/pdbsum/3wz2 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
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== Publication Abstract from PubMed == | |||
Formation 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<ref>PMID:25285636</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
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== References == | |||
<references/> | |||
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</StructureSection> | </StructureSection> | ||