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	Structural basis for aggregate dissolution and refolding by the Mycobacterium tuberculosis ClpB-DnaK bi-chaperone system.
Journal, issue, pages	Cell Rep, Vol. 35, Issue 8, Page 109166, Year 2021
Publish date	May 25, 2021
Authors	Yanting Yin / Xiang Feng / Hongjun Yu / Allison Fay / Amanda Kovach / Michael S Glickman / Huilin Li /
PubMed Abstract	The M. tuberculosis (Mtb) ClpB is a protein disaggregase that helps to rejuvenate the bacterial cell. DnaK is a protein foldase that can function alone, but it can also bind to the ClpB hexamer to ...The M. tuberculosis (Mtb) ClpB is a protein disaggregase that helps to rejuvenate the bacterial cell. DnaK is a protein foldase that can function alone, but it can also bind to the ClpB hexamer to physically couple protein disaggregation with protein refolding, although the molecular mechanism is not well understood. Here, we report the cryo-EM analysis of the Mtb ClpB-DnaK bi-chaperone in the presence of ATPγS and a protein substrate. We observe three ClpB conformations in the presence of DnaK, identify a conserved TGIP loop linking the oligonucleotide/oligosaccharide-binding domain and the nucleotide-binding domain that is important for ClpB function, derive the interface between the regulatory middle domain of the ClpB and the DnaK nucleotide-binding domain, and find that DnaK binding stabilizes, but does not bend or tilt, the ClpB middle domain. We propose a model for the synergistic actions of aggregate dissolution and refolding by the Mtb ClpB-DnaK bi-chaperone system.
External links	Cell Rep / PubMed:34038719 / PubMed Central
Methods	EM (single particle)
Resolution	3.1 - 7.0 Å
Structure data	21553 6w6e EMDB-21553: Cryo-EM map of the Mycobacterium tuberculosis ClpB disaggregase hexamer with a locally refined ClpB middle domain and a DnaK nucleotide binding domain PDB-6w6e: The Mycobacterium tuberculosis ClpB disaggregase hexamer structure with a locally refined ClpB middle domain and a DnaK nucleotide binding domain Method: EM (single particle) / Resolution: 3.7 Å 21554 6w6g EMDB-21554: Cryo-EM map of the Mycobacterium tuberculosis ClpB disaggregase hexamer in conformation I in the presence of DnaK chaperone and a model substrate PDB-6w6g: The Mycobacterium tuberculosis ClpB disaggregase hexamer structure in conformation I in the presence of DnaK chaperone and a model substrate Method: EM (single particle) / Resolution: 3.1 Å 21555 6w6h EMDB-21555: Cryo-EM map of the Mycobacterium tuberculosis ClpB disaggregase hexamer in conformation II in the presence of DnaK chaperone and a model substrate PDB-6w6h: The Mycobacterium tuberculosis ClpB disaggregase hexamer structure in conformation II in the presence of DnaK chaperone and a model substrate Method: EM (single particle) / Resolution: 3.3 Å 21556 6w6i EMDB-21556: Cryo-EM map of the Mycobacterium tuberculosis ClpB disaggregase hexamer in conformation T in the presence of DnaK chaperone and a model substrate PDB-6w6i: The Mycobacterium tuberculosis ClpB disaggregase hexamer structure in conformation T in the presence of DnaK chaperone and a model substrate Method: EM (single particle) / Resolution: 3.5 Å 21557 6w6j EMDB-21557: Cryo-EM map of the Mycobacterium tuberculosis ClpB disaggregase hexamer with a locally refined N-terminal domain in the presence of DnaK chaperone and a model substrate PDB-6w6j: The Mycobacterium tuberculosis ClpB disaggregase hexamer structure with a locally refined N-terminal domain in the presence of DnaK chaperone and a model substrate Method: EM (single particle) / Resolution: 3.2 Å 23206 7l6n EMDB-23206: CryoEM map of the Mycobacterium tuberculosis ClpB disaggregase hexamer with three locally refined ClpB middle domains and three DnaK nucleotide binding domains PDB-7l6n: The Mycobacterium tuberculosis ClpB disaggregase hexamer structure with three locally refined ClpB middle domains and three DnaK nucleotide binding domains Method: EM (single particle) / Resolution: 7.0 Å
Chemicals	ChemComp-AGS: PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER / ATP-gamma-S, energy-carrying molecule analogueYM ChemComp-ADP: ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying moleculeYM / Adenosine diphosphate
Source	mycobacterium tuberculosis (bacteria)
Keywords	CHAPERONE / ClpB-DnaK complex / Disaggregate / Unfold / Refold / ClpB/DnaK / protein aggregates / Refold protein