PDBsum entry 5vy4

Hydrolase

PDB id: 5vy4

Contents

Protein chains

(+ 8 more) 221 a.a.

(+ 8 more) 203 a.a.

PDB id:

5vy4

Name:

Hydrolase

Title:

Thermoplasma acidophilum 20s proteasome using 200kev with image shift

Structure:

Proteasome subunit alpha. Chain: a, c, e, g, i, k, m, o, q, s, u, w, y, 0. Synonym: 20s proteasome subunit a, 20s proteasome alpha subunit, proteasome core protein psma. Engineered: yes. Proteasome subunit beta. Chain: b, d, f, h, j, l, n, p, r, t, v, x, z, 1. Synonym: 20s proteasome subunit b, 20s proteasome beta subunit, proteasome core protein psmb.

Source:

Thermoplasma acidophilum. Organism_taxid: 2303. Atcc: 25905. Gene: psma, ta1288. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: psmb, ta0612. Expression_system_taxid: 562

Ensemble:

10 models

Authors:

M.A.Herzik Jr.,M.Wu,G.C.Lander

Key ref:

M.A.Herzik et al. (2017). Achieving better-than-3-Å resolution by single-particle cryo-EM at 200 keV. Nat Methods, 14, 1075-1078. PubMed id: 28991891

Date:

24-May-17 Release date: 14-Jun-17

Protein chains

P25156  (PSA_THEAC) -  Proteasome subunit alpha from Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)

Seq: 233 a.a.

Struc: 221 a.a.

Protein chains

P28061  (PSB_THEAC) -  Proteasome subunit beta from Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)

Seq: 211 a.a.

Struc: 203 a.a.

Enzyme reactions

• Enzyme class: Chains A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X, Y, Z, 0, 1: E.C.3.4.25.1 - proteasome endopeptidase complex.
• Reaction: Cleavage at peptide bonds with very broad specificity.

Nat Methods 14:1075-1078 (2017)

PubMed id: 28991891

Achieving better-than-3-Å resolution by single-particle cryo-EM at 200 keV.

M.A.Herzik, M.Wu, G.C.Lander.

ABSTRACT

Nearly all single-particle cryo-EM structures resolved to better than 4-Å resolution have been determined using 300-keV transmission electron microscopes (TEMs). We demonstrate that it is possible to obtain reconstructions of macromolecular complexes of different sizes to better than 3-Å resolution using a 200-keV TEM. These structures are of sufficient quality to unambiguously assign amino acid rotameric conformations and identify ordered water molecules.