3VR0

Crystal structure of Pyrococcus furiosus PbaB, an archaeal proteasome activator

Summary for 3VR0

• Entry DOI: 10.2210/pdb3vr0/pdb
• Related: 3GAA
• Descriptor: Putative uncharacterized protein, GOLD ION (3 entities in total)
• Functional Keywords: proteasome activator, proteasome, protein binding
• Biological source: Pyrococcus furiosus
• Total number of polymer chains: 4
• Total formula weight: 130675.01

Authors

Kumoi, K.,Satoh, T.,Hiromoto, T.,Mizushima, T.,Kamiya, Y.,Noda, M.,Uchiyama, S.,Murata, K.,Yagi, H.,Kato, K. (deposition date: 2012-04-02, release date: 2013-04-03, Last modification date: 2024-03-20)

Primary citation

Kumoi, K.,Satoh, T.,Murata, K.,Hiromoto, T.,Mizushima, T.,Kamiya, Y.,Noda, M.,Uchiyama, S.,Yagi, H.,Kato, K.
An archaeal homolog of proteasome assembly factor functions as a proteasome activator
Plos One, 8:e60294-e60294, 2013

PubMed Abstract: Assembly of the eukaryotic 20S proteasome is an ordered process involving several proteins operating as proteasome assembly factors including PAC1-PAC2 but archaeal 20S proteasome subunits can spontaneously assemble into an active cylindrical architecture. Recent bioinformatic analysis identified archaeal PAC1-PAC2 homologs PbaA and PbaB. However, it remains unclear whether such assembly factor-like proteins play an indispensable role in orchestration of proteasome subunits in archaea. We revealed that PbaB forms a homotetramer and exerts a dual function as an ATP-independent proteasome activator and a molecular chaperone through its tentacle-like C-terminal segments. Our findings provide insights into molecular evolution relationships between proteasome activators and assembly factors.

PubMed: 23555947
DOI: 10.1371/journal.pone.0060294

Experimental method

X-RAY DIFFRACTION (2.2 Å)