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- EMDB-8947: Mitochondrial peroxiredoxin from Leishmania infantum after heat s... -
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Open data
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Basic information
Entry | Database: EMDB / ID: EMD-8947 | |||||||||
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Title | Mitochondrial peroxiredoxin from Leishmania infantum after heat stress without unfolding client protein | |||||||||
![]() | Mitochondrial peroxiredoxin from Leishmania infantum after heat stress without unfolding client protein - primary map | |||||||||
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![]() | heat-shock / client-binding / holdase / unfolding / CHAPERONE | |||||||||
Function / homology | ![]() thioredoxin-dependent peroxiredoxin / thioredoxin peroxidase activity / cell redox homeostasis / hydrogen peroxide catabolic process / response to oxidative stress / mitochondrion / cytosol Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.9 Å | |||||||||
![]() | Teixeira F / Tse E | |||||||||
![]() | ![]() Title: Chaperone activation and client binding of a 2-cysteine peroxiredoxin. Authors: Filipa Teixeira / Eric Tse / Helena Castro / Karl A T Makepeace / Ben A Meinen / Christoph H Borchers / Leslie B Poole / James C Bardwell / Ana M Tomás / Daniel R Southworth / Ursula Jakob / ![]() ![]() ![]() Abstract: Many 2-Cys-peroxiredoxins (2-Cys-Prxs) are dual-function proteins, either acting as peroxidases under non-stress conditions or as chaperones during stress. The mechanism by which 2-Cys-Prxs switch ...Many 2-Cys-peroxiredoxins (2-Cys-Prxs) are dual-function proteins, either acting as peroxidases under non-stress conditions or as chaperones during stress. The mechanism by which 2-Cys-Prxs switch functions remains to be defined. Our work focuses on Leishmania infantum mitochondrial 2-Cys-Prx, whose reduced, decameric subpopulation adopts chaperone function during heat shock, an activity that facilitates the transition from insects to warm-blooded host environments. Here, we have solved the cryo-EM structure of mTXNPx in complex with a thermally unfolded client protein, and revealed that the flexible N-termini of mTXNPx form a well-resolved central belt that contacts and encapsulates the unstructured client protein in the center of the decamer ring. In vivo and in vitro cross-linking studies provide further support for these interactions, and demonstrate that mTXNPx decamers undergo temperature-dependent structural rearrangements specifically at the dimer-dimer interfaces. These structural changes appear crucial for exposing chaperone-client binding sites that are buried in the peroxidase-active protein. | |||||||||
History |
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Structure visualization
Movie |
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Structure viewer | EM map: ![]() ![]() ![]() |
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 20.8 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 10.7 KB 10.7 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 7.5 KB | Display | ![]() |
Images | ![]() | 122.1 KB | ||
Filedesc metadata | ![]() | 5.2 KB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6e0gMC ![]() 8946C ![]() 6e0fC C: citing same article ( M: atomic model generated by this map |
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Similar structure data |
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Links
EMDB pages | ![]() ![]() |
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Map
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Annotation | Mitochondrial peroxiredoxin from Leishmania infantum after heat stress without unfolding client protein - primary map | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.032 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
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Sample components
-Entire : reduced decamer form of a 2-cys peroxiredoxin after heat stress
Entire | Name: reduced decamer form of a 2-cys peroxiredoxin after heat stress |
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Components |
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-Supramolecule #1: reduced decamer form of a 2-cys peroxiredoxin after heat stress
Supramolecule | Name: reduced decamer form of a 2-cys peroxiredoxin after heat stress type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() |
-Macromolecule #1: mitochondrial 2-cys-peroxiredoxin
Macromolecule | Name: mitochondrial 2-cys-peroxiredoxin / type: protein_or_peptide / ID: 1 / Number of copies: 10 / Enantiomer: LEVO EC number: Oxidoreductases; Acting on a peroxide as acceptor; Peroxidases |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 25.400131 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MLRRLPTSCF LKRSQFRGFA ATSPLLNLDY QMYRTATVRE AAPQFSGQAV VNGAIKDINM NDYKGKYIVL FFYPMDFTFV CPTEIIAFS DRHADFEKLN TQVVAVSCDS VYSHLAWVNT PRKKGGLGEM HIPVLADKSM EIARDYGVLI EESGIALRGL F IIDKKGIL ...String: MLRRLPTSCF LKRSQFRGFA ATSPLLNLDY QMYRTATVRE AAPQFSGQAV VNGAIKDINM NDYKGKYIVL FFYPMDFTFV CPTEIIAFS DRHADFEKLN TQVVAVSCDS VYSHLAWVNT PRKKGGLGEM HIPVLADKSM EIARDYGVLI EESGIALRGL F IIDKKGIL RHSTINDLPV GRNVDEALRV LEAFQYADEN GDAIPCGWKP GQPTLDTTKA GEFFEKNM UniProtKB: thioredoxin-dependent peroxiredoxin |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Concentration | 0.2 mg/mL |
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Buffer | pH: 8 |
Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Instrument: FEI VITROBOT MARK IV |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: COUNTING / Digitization - Dimensions - Width: 3838 pixel / Digitization - Dimensions - Height: 3710 pixel / Number real images: 2368 / Average electron dose: 45.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.1 µm / Nominal defocus min: 1.2 µm / Nominal magnification: 48450 |
Sample stage | Specimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |