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
Jun 18, 2020
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Header (metadata) release
Mar 10, 2021
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Map release
Mar 10, 2021
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Update
Mar 10, 2021
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Current status
Mar 10, 2021
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)
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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: #1 Details: produced by heterologous expression, mature HSPD1, apo state
Source (natural)
Organism: Homo sapiens (human)
Recombinant expression
Organism: Escherichia coli (E. coli)
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Experimental details
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Structure determination
Method
cryo EM
Processing
single particle reconstruction
Aggregation state
particle
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Sample preparation
Concentration
2.3 mg/mL
Buffer
pH: 8
Vitrification
Cryogen name: ETHANE / Chamber humidity: 80 % / Chamber temperature: 293 K / Instrument: HOMEMADE PLUNGER / Details: blot time 0.5 s or 4 s.
Details
the inverted double ring represented a small fraction of particles (< 10 %)
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Electron microscopy
Microscope
FEI TITAN KRIOS
Image recording
Film or detector model: FEI FALCON III (4k x 4k) / Detector mode: INTEGRATING / Number grids imaged: 2 / Average exposure time: 1.5 sec. / Average electron dose: 75.0 e/Å2
Electron beam
Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron optics
Illumination mode: SPOT SCAN / Imaging mode: BRIGHT FIELD
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
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Image processing
Final reconstruction
Applied symmetry - Point group: D7 (2x7 fold dihedral) / Resolution.type: BY AUTHOR / Resolution: 4.9 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION / Number images used: 7655
Initial angle assignment
Type: MAXIMUM LIKELIHOOD / Software - Name: RELION
Final angle assignment
Type: MAXIMUM LIKELIHOOD / Software - Name: RELION
FSC plot (resolution estimation)
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