PDBsum entry 6hec

Hydrolase

PDB id: 6hec

Contents

Protein chains

(+ 8 more) 242 a.a.

(+ 8 more) 202 a.a.

(+ 0 more) 390 a.a.

Ligands

ATP ×4

ADP

Metals

_MG ×5

PDB id:

6hec

Name:

Hydrolase

Title:

Pan-proteasome in state 4

Structure:

Proteasome subunit alpha. Chain: a, a, b, b, c, c, d, d, e, e, f, f, g, g. Synonym: 20s proteasome alpha subunit,proteasome core protein psma. Engineered: yes. Mutation: yes. Proteasome subunit beta. Chain: 1, h, 2, i, 3, j, 4, k, 5, l, 6, m, 7, n. Synonym: 20s proteasome beta subunit,proteasome core protein psmb. Engineered: yes.

Source:

Archaeoglobus fulgidus (strain atcc 49558 / vc- 16 / dsm 4304 / jcm 9628 / nbrc 100126). Organism_taxid: 224325. Gene: psma, af_0490. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: psmb, af_0481. Gene: pan, af_1976. Expression_system_taxid: 562

Authors:

P.Majumder,T.Rudack,F.Beck,W.Baumeister

Key ref:

P.Majumder et al. (2019). Cryo-EM structures of the archaeal PAN-proteasome reveal an around-the-ring ATPase cycle. Proc Natl Acad Sci U S A, 116, 534-539. PubMed id: 30559193 DOI: 10.1073/pnas.1817752116

Date:

20-Aug-18 Release date: 26-Dec-18

Protein chains

O29760  (PSA_ARCFU) -  Proteasome subunit alpha from Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)

Seq: 246 a.a.

Struc: 242 a.a.

Protein chains

Q9P996  (PSB_ARCFU) -  Proteasome subunit beta from Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)

Seq: 213 a.a.

Struc: 202 a.a.

Protein chains

O28303  (PAN_ARCFU) -  Proteasome-activating nucleotidase from Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)

Seq: 398 a.a.

Struc: 390 a.a.

Enzyme reactions

• Enzyme class 1: Chains A, a, B, b, C, c, D, d, E, e, F, f, G, g, 1, h, 2, i, 3, j, 4, k, 5, l, 6, m, 7, n: E.C.3.4.25.1 - proteasome endopeptidase complex.
• Reaction: Cleavage at peptide bonds with very broad specificity.
• Enzyme class 2: Chains H, I, K, L, M, J: E.C.?

Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

DOI no: 10.1073/pnas.1817752116

Proc Natl Acad Sci U S A 116:534-539 (2019)

PubMed id: 30559193

Cryo-EM structures of the archaeal PAN-proteasome reveal an around-the-ring ATPase cycle.

P.Majumder, T.Rudack, F.Beck, R.Danev, G.Pfeifer, I.Nagy, W.Baumeister.

ABSTRACT

Proteasomes occur in all three domains of life, and are the principal molecular machines for the regulated degradation of intracellular proteins. They play key roles in the maintenance of protein homeostasis, and control vital cellular processes. While the eukaryotic 26S proteasome is extensively characterized, its putative evolutionary precursor, the archaeal proteasome, remains poorly understood. The primordial archaeal proteasome consists of a 20S proteolytic core particle (CP), and an AAA-ATPase module. This minimal complex degrades protein unassisted by non-ATPase subunits that are present in a 26S proteasome regulatory particle (RP). Using cryo-EM single-particle analysis, we determined structures of the archaeal CP in complex with the AAA-ATPase PAN (proteasome-activating nucleotidase). Five conformational states were identified, elucidating the functional cycle of PAN, and its interaction with the CP. Coexisting nucleotide states, and correlated intersubunit signaling features, coordinate rotation of the PAN-ATPase staircase, and allosterically regulate N-domain motions and CP gate opening. These findings reveal the structural basis for a sequential around-the-ring ATPase cycle, which is likely conserved in AAA-ATPases.