PDBsum entry 3whk

Hydrolase

PDB id: 3whk

Contents

Protein chains

(+ 2 more) 248 a.a.

Ligands

ATP ×8

Waters ×83

PDB id:

3whk

Name:

Hydrolase

Title:

Crystal structure of pan-rpt5c chimera

Structure:

Proteasome-activating nucleotidase, 26s protease regulatory subunit 6a. Chain: a, b, c, d, e, f, g, h. Synonym: pan, proteasomal atpase, proteasome regulatory atpase, proteasome regulatory particle, tat-binding protein homolog 1, tbp-1. Engineered: yes. Other_details: fusion protein of residues 125-309 from proteasome- activating nucleotidase (pan, unp q8u4h3), linker (ef), and residues 356-434 from 26s protease regulatory subunit 6a (rpt5, unp p33297).

Source:

Pyrococcus furiosus, saccharomyces cerevisiae. Yeast. Organism_taxid: 186497, 559292. Strain: dsm 3638, s288c. Gene: pan, pf0115, o3258, rpt5, yor117w, yor3258w, yta1. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.60Å R-factor: 0.243 R-free: 0.275

Authors:

T.Satoh,Y.Saeki,T.Hiromoto,Y.-H.Wang,Y.Uekusa,H.Yagi,H.Yoshihara, M.Yagi-Utsumi,T.Mizushima,K.Tanaka,K.Kato

Key ref:

T.Satoh et al. (2014). Structural basis for proteasome formation controlled by an assembly chaperone nas2. Structure, 22, 731-743. PubMed id: 24685148 DOI: 10.1016/j.str.2014.02.014

Date:

26-Aug-13 Release date: 26-Mar-14

Protein chains

P33297  (PRS6A_YEAST) -  26S proteasome regulatory subunit 6A from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 434 a.a.

Struc: 248 a.a.*

Protein chains

Q8U4H3  (PAN_PYRFU) -  Proteasome-activating nucleotidase from Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)

Seq: 396 a.a.

Struc: 248 a.a.*

* PDB and UniProt seqs differ at 120 residue positions (black crosses)

DOI no: 10.1016/j.str.2014.02.014

Structure 22:731-743 (2014)

PubMed id: 24685148

Structural basis for proteasome formation controlled by an assembly chaperone nas2.

T.Satoh, Y.Saeki, T.Hiromoto, Y.H.Wang, Y.Uekusa, H.Yagi, H.Yoshihara, M.Yagi-Utsumi, T.Mizushima, K.Tanaka, K.Kato.

ABSTRACT

Proteasome formation does not occur due to spontaneous self-organization but results from a highly ordered process assisted by several assembly chaperones. The assembly of the proteasome ATPase subunits is assisted by four client-specific chaperones, of which three have been structurally resolved. Here, we provide the structural basis for the working mechanisms of the last, hereto structurally uncharacterized assembly chaperone, Nas2. We revealed that Nas2 binds to the Rpt5 subunit in a bivalent mode: the N-terminal helical domain of Nas2 masks the Rpt1-interacting surface of Rpt5, whereas its C-terminal PDZ domain caps the C-terminal proteasome-activating motif. Thus, Nas2 operates as a proteasome activation blocker, offering a checkpoint during the formation of the 19S ATPase prior to its docking onto the proteolytic 20S core particle.