Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Structure and conformational cycle of a bacteriophage-encoded chaperonin.
Journal, issue, pages	PLoS One, Vol. 15, Issue 4, Page e0230090, Year 2020
Publish date	Apr 27, 2020
Authors	Andreas Bracher / Simanta S Paul / Huping Wang / Nadine Wischnewski / F Ulrich Hartl / Manajit Hayer-Hartl /
PubMed 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 ...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.
External links	PLoS One / PubMed:32339190 / PubMed Central
Methods	EM (single particle) / X-ray diffraction
Resolution	3.45 - 5.91 Å
Structure data	10528 6tmv EMDB-10528, PDB-6tmv: Structure of the chaperonin gp146 from the bacteriophage EL (Pseudomonas aeruginosa) in the apo state Method: EM (single particle) / Resolution: 3.45 Å 10529 6tmw EMDB-10529, PDB-6tmw: Structure of the chaperonin gp146 from the bacteriophage EL (Pseudomonas aeruginosa) in complex with ADP Method: EM (single particle) / Resolution: 5.91 Å 10530 6tmx EMDB-10530, PDB-6tmx: Structure of the chaperonin gp146 from the bacteriophage EL (Pseudomonas aeruginosa) in complex with ATPgammaS Method: EM (single particle) / Resolution: 5.8 Å PDB-6tmt: Crystal structure of the chaperonin gp146 from the bacteriophage EL 2 (Pseudomonas aeruginosa) in presence of ATP-BeFx, crystal form I Method: X-RAY DIFFRACTION / Resolution: 4.03 Å PDB-6tmu: Crystal structure of the chaperonin gp146 from the bacteriophage EL 2 (Pseudomonas aeruginosa) in presence of ATP-BeFx, crystal form II Method: X-RAY DIFFRACTION / Resolution: 3.54 Å
Chemicals	ChemComp-MG: Unknown entry ChemComp-ATP: ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying moleculeYM ChemComp-K: Unknown entry ChemComp-ADP: ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying moleculeYM ChemComp-AGS: PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER / ATP-gamma-S, energy-carrying molecule analogue*YM
Source	pseudomonas phage el (virus)
Keywords	CHAPERONE / molecular chaperone / ATPase / chaperonin