Biotechnology and Biological Sciences Research Council (BBSRC)
BB/P026397/1
United Kingdom
Wellcome Trust
108466/Z/15/Z
United Kingdom
Citation
Journal: iScience / Year: 2021 Title: Cryo-EM structure of human mitochondrial HSPD1. Authors: David P Klebl / Matthew C Feasey / Emma L Hesketh / Neil A Ranson / Heiko Wurdak / Frank Sobott / Robin S Bon / Stephen P Muench / Abstract: Chaperonins play an important role in folding newly synthesized or translocated proteins in all organisms. The bacterial chaperonin GroEL has served as a model system for the understanding of these ...Chaperonins play an important role in folding newly synthesized or translocated proteins in all organisms. The bacterial chaperonin GroEL has served as a model system for the understanding of these proteins. In comparison, its human homolog, known as mitochondrial heat shock protein family member D1 (HSPD1) is poorly understood. Here, we present the structure of HSPD1 in the apo state determined by cryo-electron microscopy (cryo-EM). Unlike GroEL, HSPD1 forms mostly single ring assemblies in the absence of co-chaperonin (HSPE1). Comparison with GroEL shows a rotation and increased flexibility of the apical domain. Together with published structures of the HSPD1/HSPE1 co-chaperonin complex, this work gives insight into the structural changes that occur during the catalytic cycle. This new understanding of HSPD1 structure and its rearrangements upon complex formation may provide new insights for the development of HSPD1-targeting treatments against a diverse range of diseases including glioblastoma.
History
Deposition
Nov 17, 2020
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Header (metadata) release
Feb 10, 2021
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Map release
Feb 10, 2021
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Update
May 1, 2024
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Current status
May 1, 2024
Processing site: PDBe / Status: Released
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Structure visualization
Movie
Surface view with section colored by density value
Entire : human mitochondrial heat shock protein family member D1 (HSPD1)
Entire
Name: human mitochondrial heat shock protein family member D1 (HSPD1)
Components
Complex: human mitochondrial heat shock protein family member D1 (HSPD1)
Protein or peptide: 60 kDa heat shock protein, mitochondrial
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Supramolecule #1: human mitochondrial heat shock protein family member D1 (HSPD1)
Supramolecule
Name: human mitochondrial heat shock protein family member D1 (HSPD1) type: complex / ID: 1 / Parent: 0 / Macromolecule list: all Details: produced by heterologous expression, mature HSPD1, apo state
Cryogen name: ETHANE / Chamber humidity: 90 % / Chamber temperature: 293 K / Instrument: FEI VITROBOT MARK IV / Details: blot time 6 s blot force 6.
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Electron microscopy
Microscope
FEI TITAN KRIOS
Image recording
Film or detector model: FEI FALCON III (4k x 4k) / Detector mode: COUNTING / Number grids imaged: 1 / Average exposure time: 70.0 sec. / Average electron dose: 38.5 e/Å2
Electron beam
Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron optics
Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
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Image processing
Startup model
Type of model: NONE
Final reconstruction
Resolution.type: BY AUTHOR / Resolution: 3.5 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION / Number images used: 124784
Initial angle assignment
Type: MAXIMUM LIKELIHOOD / Software - Name: RELION
Final angle assignment
Type: MAXIMUM LIKELIHOOD / Software - Name: RELION
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