3WZ2

Crystal structure of Pyrococcus furiosus PbaA, an archaeal homolog of proteasome-assembly chaperone

Summary for 3WZ2

• Entry DOI: 10.2210/pdb3wz2/pdb
• Related: 3GAA 3VR0
• Descriptor: Uncharacterized protein (2 entities in total)
• Functional Keywords: proteasome, proteasome activator, proteasome assembly chaperone, chaperone
• Biological source: Pyrococcus furiosus DSM 3638
• Total number of polymer chains: 5
• Total formula weight: 136924.13

Authors

Sikdar, A.,Satoh, T.,Kawasaki, M.,Kato, K. (deposition date: 2014-09-18, release date: 2014-10-08, Last modification date: 2024-03-20)

Primary citation

Sikdar, A.,Satoh, T.,Kawasaki, M.,Kato, K.
Crystal structure of archaeal homolog of proteasome-assembly chaperone PbaA
Biochem.Biophys.Res.Commun., 453:493-497, 2014

PubMed Abstract: 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-Å 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.

PubMed: 25285636
DOI: 10.1016/j.bbrc.2014.09.114

Experimental method

X-RAY DIFFRACTION (2.25 Å)