3wz2 | pdb_00003wz2

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

spinqualitylabelsall models 3wz2, resolution 2.25Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3wz2 is a 5 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 3vr0, 3gaa Resources: FirstGlance, OCA, RCSB, PDBsum 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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