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- EMDB-11950: Structure of the human mitochondrial HSPD1 single ring -

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Basic information

Entry
Database: EMDB / ID: EMD-11950
TitleStructure of the human mitochondrial HSPD1 single ring
Map datafinal map filtered by local resolution
Sample
  • Complex: human mitochondrial heat shock protein family member D1 (HSPD1)
    • Protein or peptide: 60 kDa heat shock protein, mitochondrial
KeywordsHSPD1 / Hsp60 / chaperonin / CHAPERONE
Function / homology
Function and homology information


coated vesicle / isotype switching to IgG isotypes / mitochondrial unfolded protein response / TFAP2A acts as a transcriptional repressor during retinoic acid induced cell differentiation / apolipoprotein A-I binding / lipopolysaccharide receptor complex / protein import into mitochondrial intermembrane space / migrasome / high-density lipoprotein particle binding / positive regulation of T cell mediated immune response to tumor cell ...coated vesicle / isotype switching to IgG isotypes / mitochondrial unfolded protein response / TFAP2A acts as a transcriptional repressor during retinoic acid induced cell differentiation / apolipoprotein A-I binding / lipopolysaccharide receptor complex / protein import into mitochondrial intermembrane space / migrasome / high-density lipoprotein particle binding / positive regulation of T cell mediated immune response to tumor cell / Mitochondrial protein import / chaperonin ATPase / positive regulation of macrophage activation / cellular response to interleukin-7 / biological process involved in interaction with symbiont / MyD88-dependent toll-like receptor signaling pathway / sperm plasma membrane / 'de novo' protein folding / B cell proliferation / DNA replication origin binding / apolipoprotein binding / B cell activation / positive regulation of interferon-alpha production / protein maturation / apoptotic mitochondrial changes / positive regulation of interleukin-10 production / response to unfolded protein / chaperone-mediated protein complex assembly / clathrin-coated pit / sperm midpiece / Mitochondrial protein degradation / positive regulation of interleukin-12 production / response to cold / T cell activation / secretory granule / isomerase activity / lipopolysaccharide binding / ATP-dependent protein folding chaperone / : / positive regulation of interleukin-6 production / positive regulation of type II interferon production / double-stranded RNA binding / positive regulation of T cell activation / unfolded protein binding / p53 binding / protein folding / protein-folding chaperone binding / single-stranded DNA binding / protein refolding / mitochondrial inner membrane / early endosome / protein stabilization / mitochondrial matrix / positive regulation of apoptotic process / ubiquitin protein ligase binding / negative regulation of apoptotic process / enzyme binding / cell surface / ATP hydrolysis activity / protein-containing complex / mitochondrion / RNA binding / extracellular space / extracellular exosome / ATP binding / membrane / plasma membrane / cytosol / cytoplasm
Similarity search - Function
Chaperonin Cpn60, conserved site / Chaperonins cpn60 signature. / Chaperonin Cpn60/GroEL / GroEL-like equatorial domain superfamily / TCP-1-like chaperonin intermediate domain superfamily / GroEL-like apical domain superfamily / TCP-1/cpn60 chaperonin family / Chaperonin Cpn60/GroEL/TCP-1 family
Similarity search - Domain/homology
60 kDa heat shock protein, mitochondrial
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.5 Å
AuthorsKlebl DP / Feasey MC / Muench SP
Funding support United Kingdom, 2 items
OrganizationGrant numberCountry
Biotechnology and Biological Sciences Research Council (BBSRC)BB/P026397/1 United Kingdom
Wellcome Trust108466/Z/15/Z United Kingdom
CitationJournal: 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
DepositionNov 17, 2020-
Header (metadata) releaseFeb 10, 2021-
Map releaseFeb 10, 2021-
UpdateMay 1, 2024-
Current statusMay 1, 2024Processing site: PDBe / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.05
  • Imaged by UCSF Chimera
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  • Surface view colored by cylindrical radius
  • Surface level: 0.05
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  • Surface view with fitted model
  • Atomic models: PDB-7azp
  • Surface level: 0.05
  • Imaged by UCSF Chimera
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Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_11950.png

Downloads & links

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Map

FileDownload / File: emd_11950.map.gz / Format: CCP4 / Size: 64 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Annotationfinal map filtered by local resolution
Projections & slices

Image control

Size
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Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.07 Å/pix.
x 256 pix.
= 272.64 Å		1.07 Å/pix.
x 256 pix.
= 272.64 Å		1.07 Å/pix.
x 256 pix.
= 272.64 Å

Surface

Projections

Slices (1/3)

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Images are generated by Spider.

Voxel sizeX=Y=Z: 1.065 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.05 / Movie #1: 0.05
Minimum - Maximum-0.12929067 - 0.32589114
Average (Standard dev.)0.00015628578 (±0.009971453)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions256256256
Spacing256256256
CellA=B=C: 272.64 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.0651.0651.065
M x/y/z256256256
origin x/y/z0.0000.0000.000
length x/y/z272.640272.640272.640
α/β/γ90.00090.00090.000
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS256256256
D min/max/mean-0.1290.3260.000

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Supplemental data

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Additional map: unsharpened map

Fileemd_11950_additional_1.map
Annotationunsharpened map
Projections & Slices
AxesZYX

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Half map: #2

Fileemd_11950_half_map_1.map
Projections & Slices
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Histogram

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Half map: #1

Fileemd_11950_half_map_2.map
Projections & Slices
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Sample components

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Entire : human mitochondrial heat shock protein family member D1 (HSPD1)

EntireName: 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)

SupramoleculeName: 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
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: 60 kDa heat shock protein, mitochondrial

MacromoleculeName: 60 kDa heat shock protein, mitochondrial / type: protein_or_peptide / ID: 1 / Number of copies: 7 / Enantiomer: LEVO / EC number: chaperonin ATPase
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 58.306977 KDa
Recombinant expressionOrganism: Escherichia coli BL21 (bacteria)
SequenceString: SNAAKDVKFG ADARALMLQG VDLLADAVAV TMGPKGRTVI IEQSWGSPKV TKDGVTVAKS IDLKDKYKNI GAKLVQDVAN NTNEEAGDG TTTATVLARS IAKEGFEKIS KGANPVEIRR GVMLAVDAVI AELKKQSKPV TTPEEIAQVA TISANGDKEI G NIISDAMK ...String:
SNAAKDVKFG ADARALMLQG VDLLADAVAV TMGPKGRTVI IEQSWGSPKV TKDGVTVAKS IDLKDKYKNI GAKLVQDVAN NTNEEAGDG TTTATVLARS IAKEGFEKIS KGANPVEIRR GVMLAVDAVI AELKKQSKPV TTPEEIAQVA TISANGDKEI G NIISDAMK KVGRKGVITV KDGKTLNDEL EIIEGMKFDR GYISPYFINT SKGQKCEFQD AYVLLSEKKI SSIQSIVPAL EI ANAHRKP LVIIAEDVDG EALSTLVLNR LKVGLQVVAV KAPGFGDNRK NQLKDMAIAT GGAVFGEEGL TLNLEDVQPH DLG KVGEVI VTKDDAMLLK GKGDKAQIEK RIQEIIEQLD VTTSEYEKEK LNERLAKLSD GVAVLKVGGT SDVEVNEKKD RVTD ALNAT RAAVEEGIVL GGGCALLRCI PALDSLTPAN EDQKIGIEII KRTLKIPAMT IAKNAGVEGS LIVEKIMQSS SEVGY DAMA GDFVNMVEKG IIDPTKVVRT ALLDAAGVAS LLTTAEVVVT EIPKEEKDPG MGAMGGMGGG MGGGMF

UniProtKB: 60 kDa heat shock protein, mitochondrial

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

Concentration2.3 mg/mL
BufferpH: 7.7
VitrificationCryogen 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

MicroscopeFEI TITAN KRIOS
Image recordingFilm 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 beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: NONE
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.5 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION / Number images used: 124784
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION
FSC plot (resolution estimation)

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Atomic model buiding 1

Initial model
PDB IDChain

1xck

source_name: PDB, initial_model_type: experimental model

4pj1

source_name: PDB, initial_model_type: experimental model
RefinementSpace: REAL / Protocol: OTHER
Output model

PDB-7azp:
Structure of the human mitochondrial HSPD1 single ring

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