› 6tmt

X-ray diffraction
4.03Å resolution

Crystal structure of the chaperonin gp146 from the bacteriophage EL 2 (Pseudomonas aeruginosa) in presence of ATP-BeFx, crystal form I

Released:
DOI: 10.2210/pdb6tmt/pdb
PDB entry 6tmt coloured by chain, front view.
PDB entry 6tmt coloured by chain, side view.
PDB entry 6tmt coloured by chain, top view.
Source organism: Pseudomonas phage EL
Primary publication:
Structure and conformational cycle of a bacteriophage-encoded chaperonin.
Bracher A, Paul SS, Wang H, Wischnewski N, Hartl FU, Hayer-Hartl M
OpenAccess logo PLoS One 15 e0230090 (2020)
PMID: 32339190

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo heptamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-174223 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Putative GroEL-like chaperonine protein Chains: A, B, C, D, E, F, G
Molecule details ›
Chains: A, B, C, D, E, F, G
Length: 558 amino acids
Theoretical weight: 61.76 KDa
Source organism: Pseudomonas phage EL
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q2Z0T5 (Residues: 1-558; Coverage: 100%)
Sequence domains: TCP-1/cpn60 chaperonin family

Ligands and Environments

2 bound ligands:
Ligand MG 7 x MG
Ligand ATP 7 x ATP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID30B
Spacegroup: P212121
Unit cell:
a: 137.92Å b: 149.427Å c: 268.83Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.258 0.256 0.299
Expression system: Escherichia coli BL21(DE3)

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Citations

1 review citation

Creating de novo peptide-based bioactivities: from assembly to origami.
Ma et al. (2022)
3 other articles