PDBsum entry 6tmt

Chaperone

PDB id: 6tmt

Contents

Protein chains

(+ 1 more) 545 a.a.

Ligands

ATP ×7

Metals

_MG ×7

PDB id:

6tmt

Name:

Chaperone

Title:

Crystal structure of the chaperonin gp146 from the bacteriophage el 2 (pseudomonas aeruginosa) in presence of atp-befx, crystal form i

Structure:

Putative groel-like chaperonine protein. Chain: a, b, c, d, e, f, g. Engineered: yes

Source:

Pseudomonas phage el. Organism_taxid: 273133. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

Resolution:

4.03Å R-factor: 0.258 R-free: 0.299

Authors:

A.Bracher,S.S.Paul,H.Wang,N.Wischnewski,F.U.Hartl,M.Hayer-Hartl

Key ref:

A.Bracher et al. (2020). Structure and conformational cycle of a bacteriophage-encoded chaperonin. PLoS One, 15, e0230090. PubMed id: 32339190 DOI: 10.1371/journal.pone.0230090

Date:

05-Dec-19 Release date: 22-Apr-20

Protein chains

Q2Z0T5  (Q2Z0T5_9CAUD) -  Putative GroEL-like chaperonine protein from Pseudomonas phage EL

Seq: 558 a.a.

Struc: 545 a.a.

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1371/journal.pone.0230090

PLoS One 15:e0230090 (2020)

PubMed id: 32339190

Structure and conformational cycle of a bacteriophage-encoded chaperonin.

A.Bracher, S.S.Paul, H.Wang, N.Wischnewski, F.U.Hartl, M.Hayer-Hartl.

ABSTRACT

Chaperonins are ubiquitous molecular chaperones found in all domains of life. They form ring-shaped complexes that assist in the folding of substrate proteins in an ATP-dependent reaction cycle. Key to the folding cycle is the transient encapsulation of substrate proteins by the chaperonin. Here we present a structural and functional characterization of the chaperonin gp146 (ɸEL) from the phage EL of Pseudomonas aeruginosa. ɸEL, an evolutionarily distant homolog of bacterial GroEL, is active in ATP hydrolysis and prevents the aggregation of denatured protein in a nucleotide-dependent manner. However, ɸEL failed to refold the encapsulation-dependent model substrate rhodanese and did not interact with E. coli GroES, the lid-shaped co-chaperone of GroEL. ɸEL forms tetradecameric double-ring complexes, which dissociate into single rings in the presence of ATP. Crystal structures of ɸEL (at 3.54 and 4.03 Å) in presence of ATP•BeFx revealed two distinct single-ring conformational states, both with open access to the ring cavity. One state showed uniform ATP-bound subunit conformations (symmetric state), whereas the second combined distinct ATP- and ADP-bound subunit conformations (asymmetric state). Cryo-electron microscopy of apo-ɸEL revealed a double-ring structure composed of rings in the asymmetric state (3.45 Å resolution). We propose that the phage chaperonin undergoes nucleotide-dependent conformational switching between double- and single rings and functions in aggregation prevention without substrate protein encapsulation. Thus, ɸEL may represent an evolutionarily more ancient chaperonin prior to acquisition of the encapsulation mechanism.