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	CryoEM reveals the stochastic nature of individual ATP binding events in a group II chaperonin.
Journal, issue, pages	Nat Commun, Vol. 12, Issue 1, Page 4754, Year 2021
Publish date	Aug 6, 2021
Authors	Yanyan Zhao / Michael F Schmid / Judith Frydman / Wah Chiu /
PubMed Abstract	Chaperonins are homo- or hetero-oligomeric complexes that use ATP binding and hydrolysis to facilitate protein folding. ATP hydrolysis exhibits both positive and negative cooperativity. The mechanism ...Chaperonins are homo- or hetero-oligomeric complexes that use ATP binding and hydrolysis to facilitate protein folding. ATP hydrolysis exhibits both positive and negative cooperativity. The mechanism by which chaperonins coordinate ATP utilization in their multiple subunits remains unclear. Here we use cryoEM to study ATP binding in the homo-oligomeric archaeal chaperonin from Methanococcus maripaludis (MmCpn), consisting of two stacked rings composed of eight identical subunits each. Using a series of image classification steps, we obtained different structural snapshots of individual chaperonins undergoing the nucleotide binding process. We identified nucleotide-bound and free states of individual subunits in each chaperonin, allowing us to determine the ATP occupancy state of each MmCpn particle. We observe distinctive tertiary and quaternary structures reflecting variations in nucleotide occupancy and subunit conformations in each chaperonin complex. Detailed analysis of the nucleotide distribution in each MmCpn complex indicates that individual ATP binding events occur in a statistically random manner for MmCpn, both within and across the rings. Our findings illustrate the power of cryoEM to characterize a biochemical property of multi-subunit ligand binding cooperativity at the individual particle level.
External links	Nat Commun / PubMed:34362932 / PubMed Central
Methods	EM (single particle)
Resolution	3.9 - 6.4 Å
Structure data	24324 7r9e EMDB-24324, PDB-7r9e: Methanococcus maripaludis chaperonin, open conformation 1 Method: EM (single particle) / Resolution: 4.0 Å 24325 7r9h EMDB-24325, PDB-7r9h: Methanococcus maripaludis chaperonin, open conformation 2 Method: EM (single particle) / Resolution: 6.3 Å 24326 7r9i EMDB-24326, PDB-7r9i: Methanococcus maripaludis chaperonin, open conformation 2 Method: EM (single particle) / Resolution: 6.4 Å 24327 7r9j EMDB-24327, PDB-7r9j: Methanococcus maripaludis chaperonin, open conformation 4 Method: EM (single particle) / Resolution: 6.3 Å 24328 7r9k EMDB-24328, PDB-7r9k: Methanococcus maripaludis chaperonin, closed conformation 4 Method: EM (single particle) / Resolution: 4.1 Å 24329 7r9m EMDB-24329, PDB-7r9m: Methanococcus maripaludis chaperonin, closed conformation 2 Method: EM (single particle) / Resolution: 4.0 Å 24330 7r9o EMDB-24330, PDB-7r9o: Methanococcus maripaludis chaperonin, closed conformation 1 Method: EM (single particle) / Resolution: 4.0 Å 24331 7r9u EMDB-24331, PDB-7r9u: Methanococcus maripaludis chaperonin, closed conformation 3 Method: EM (single particle) / Resolution: 4.4 Å 24363 7rak EMDB-24363, PDB-7rak: Methanococcus maripaludis chaperonin complex in open conformation Method: EM (single particle) / Resolution: 3.9 Å
Chemicals	ChemComp-ATP: ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM
Source	methanococcus maripaludis (archaea)
Keywords	CHAPERONE / Open conformation / Closed conformation / Complex / chaperonin.