|Entry||Database: EMDB / ID: 9027|
|Title||Mtb ClpB in complex with ATPgammaS and casein, Combined|
|Map data||Mtb ClpB in complex with ATPgammaS and casein, Combined|
|Sample||Mtb ClpB in complex with ATPgammaS and casein:|
|Source||Mycobacterium tuberculosis (bacteria)|
|Method||single particle reconstruction / cryo EM / 3.6 Å resolution|
|Authors||Yu HJ / Li HL|
|Citation||Journal: Proc. Natl. Acad. Sci. U.S.A. / Year: 2018|
Title: ATP hydrolysis-coupled peptide translocation mechanism of ClpB.
Authors: Hongjun Yu / Tania J Lupoli / Amanda Kovach / Xing Meng / Gongpu Zhao / Carl F Nathan / Huilin Li
Abstract: The protein disaggregase ClpB hexamer is conserved across evolution and has two AAA+-type nucleotide-binding domains, NBD1 and NBD2, in each protomer. In (), ClpB facilitates asymmetric distribution ...The protein disaggregase ClpB hexamer is conserved across evolution and has two AAA+-type nucleotide-binding domains, NBD1 and NBD2, in each protomer. In (), ClpB facilitates asymmetric distribution of protein aggregates during cell division to help the pathogen survive and persist within the host, but a mechanistic understanding has been lacking. Here we report cryo-EM structures at 3.8- to 3.9-Å resolution of ClpB bound to a model substrate, casein, in the presence of the weakly hydrolyzable ATP mimic adenosine 5'-[γ-thio]triphosphate. ClpB existed in solution in two closed-ring conformations, conformers 1 and 2. In both conformers, the 12 pore-loops on the 12 NTDs of the six protomers (P1-P6) were arranged similarly to a staircase around the bound peptide. Conformer 1 is a low-affinity state in which three of the 12 pore-loops (the protomer P1 NBD1 and NBD2 loops and the protomer P2 NBD1 loop) are not engaged with peptide. Conformer 2 is a high-affinity state because only one pore-loop (the protomer P2 NBD1 loop) is not engaged with the peptide. The resolution of the two conformations, along with their bound substrate peptides and nucleotides, enabled us to propose a nucleotide-driven peptide translocation mechanism of a bacterial ClpB that is largely consistent with several recent unfoldase structures, in particular with the eukaryotic Hsp104. However, whereas Hsp104's two NBDs move in opposing directions during one step of peptide translocation, in Mtb ClpB the two NBDs move only in the direction of translocation.
|Date||Deposition: Aug 6, 2018 / Header (metadata) release: Sep 26, 2018 / Map release: Sep 26, 2018 / Last update: Dec 5, 2018|
|Structure viewer||EM map: |
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|File||emd_9027.map.gz (map file in CCP4 format, 99589 KB)|
|Projections & slices|
Images are generated by Spider.
|Voxel size||X=Y=Z: 1.074 Å|
CCP4 map header:
-Entire Mtb ClpB in complex with ATPgammaS and casein
|Entire||Name: Mtb ClpB in complex with ATPgammaS and casein / Number of components: 1|
-Component #1: protein, Mtb ClpB in complex with ATPgammaS and casein
|Protein||Name: Mtb ClpB in complex with ATPgammaS and casein / Recombinant expression: No|
|Source||Species: Mycobacterium tuberculosis (bacteria)|
|Source (engineered)||Expression System: Escherichia coli (E. coli)|
|Specimen||Specimen state: particle / Method: cryo EM|
|Sample solution||pH: 7.5|
|Vitrification||Cryogen name: ETHANE|
-Electron microscopy imaging
Model: Titan Krios / Image courtesy: FEI Company
|Imaging||Microscope: FEI TITAN KRIOS|
|Electron gun||Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Electron dose: 1.7 e/Å2 / Illumination mode: FLOOD BEAM|
|Lens||Imaging mode: BRIGHT FIELD|
|Specimen Holder||Model: OTHER|
|Camera||Detector: GATAN K2 SUMMIT (4k x 4k)|
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