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Yorodumi- PDB-8k17: Human collagen prolyl processing enzyme complex, P3H1/CRTAP/PPIB ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 8k17 | |||||||||
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Title | Human collagen prolyl processing enzyme complex, P3H1/CRTAP/PPIB heterotrimer, bound to collagen alpha-1(I) chain | |||||||||
Components |
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Keywords | CYTOSOLIC PROTEIN / complex / hydroxylase / collagen / ER protein | |||||||||
Function / homology | Function and homology information procollagen-proline 3-dioxygenase / procollagen-proline 3-dioxygenase activity / protein hydroxylation / negative regulation of post-translational protein modification / endoplasmic reticulum chaperone complex / positive regulation by host of viral genome replication / Collagen biosynthesis and modifying enzymes / collagen metabolic process / positive regulation by host of viral process / positive regulation of multicellular organism growth ...procollagen-proline 3-dioxygenase / procollagen-proline 3-dioxygenase activity / protein hydroxylation / negative regulation of post-translational protein modification / endoplasmic reticulum chaperone complex / positive regulation by host of viral genome replication / Collagen biosynthesis and modifying enzymes / collagen metabolic process / positive regulation by host of viral process / positive regulation of multicellular organism growth / collagen fibril organization / L-ascorbic acid binding / RNA polymerase binding / cyclosporin A binding / regulation of protein secretion / protein peptidyl-prolyl isomerization / smooth endoplasmic reticulum / chaperone-mediated protein folding / neutrophil chemotaxis / bone development / peptidylprolyl isomerase / peptidyl-prolyl cis-trans isomerase activity / positive regulation of neuron projection development / SARS-CoV-1 activates/modulates innate immune responses / unfolded protein binding / melanosome / protein folding / spermatogenesis / protein stabilization / iron ion binding / negative regulation of cell population proliferation / endoplasmic reticulum lumen / intracellular membrane-bounded organelle / focal adhesion / perinuclear region of cytoplasm / endoplasmic reticulum / protein-containing complex / RNA binding / extracellular space / extracellular exosome / nucleoplasm / membrane / nucleus / cytosol / cytoplasm Similarity search - Function | |||||||||
Biological species | Homo sapiens (human) | |||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.18 Å | |||||||||
Authors | Li, W. / Peng, J. / Yao, D. / Rao, B. / Xia, Y. / Wang, Q. / Li, S. / Cao, M. / Shen, Y. / Ma, P. ...Li, W. / Peng, J. / Yao, D. / Rao, B. / Xia, Y. / Wang, Q. / Li, S. / Cao, M. / Shen, Y. / Ma, P. / Liao, R. / Qin, A. / Zhao, J. / Cao, Y. | |||||||||
Funding support | China, 2items
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Citation | Journal: Nat Commun / Year: 2024 Title: The structural basis for the collagen processing by human P3H1/CRTAP/PPIB ternary complex. Authors: Wenguo Li / Junjiang Peng / Deqiang Yao / Bing Rao / Ying Xia / Qian Wang / Shaobai Li / Mi Cao / Yafeng Shen / Peixiang Ma / Rijing Liao / An Qin / Jie Zhao / Yu Cao / Abstract: Collagen posttranslational processing is crucial for its proper assembly and function. Disruption of collagen processing leads to tissue development and structure disorders like osteogenesis ...Collagen posttranslational processing is crucial for its proper assembly and function. Disruption of collagen processing leads to tissue development and structure disorders like osteogenesis imperfecta (OI). OI-related collagen processing machinery includes prolyl 3-hydroxylase 1 (P3H1), peptidyl-prolyl cis-trans isomerase B (PPIB), and cartilage-associated protein (CRTAP), with their structural organization and mechanism unclear. We determine cryo-EM structures of the P3H1/CRTAP/PPIB complex. The active sites of P3H1 and PPIB form a face-to-face bifunctional reaction center, indicating a coupled modification mechanism. The structure of the P3H1/CRTAP/PPIB/collagen peptide complex reveals multiple binding sites, suggesting a substrate interacting zone. Unexpectedly, a dual-ternary complex is observed, and the balance between ternary and dual-ternary states can be altered by mutations in the P3H1/PPIB active site and the addition of PPIB inhibitors. These findings provide insights into the structural basis of collagen processing by P3H1/CRTAP/PPIB and the molecular pathology of collagen-related disorders. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 8k17.cif.gz | 258.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb8k17.ent.gz | 201.5 KB | Display | PDB format |
PDBx/mmJSON format | 8k17.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 8k17_validation.pdf.gz | 1.1 MB | Display | wwPDB validaton report |
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Full document | 8k17_full_validation.pdf.gz | 1.1 MB | Display | |
Data in XML | 8k17_validation.xml.gz | 42.8 KB | Display | |
Data in CIF | 8k17_validation.cif.gz | 64.9 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/k1/8k17 ftp://data.pdbj.org/pub/pdb/validation_reports/k1/8k17 | HTTPS FTP |
-Related structure data
Related structure data | 36787MC 8k0eC 8k0fC 8k0iC 8k0mC 8kc9C M: map data used to model this data C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
-Assembly
Deposited unit |
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1 |
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-Components
-Protein , 3 types, 3 molecules ABC
#1: Protein | Mass: 83485.727 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: P3H1, GROS1, LEPRE1, PSEC0109 / Production host: Homo sapiens (human) References: UniProt: Q32P28, procollagen-proline 3-dioxygenase |
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#2: Protein | Mass: 50749.184 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: CRTAP, CASP / Production host: Homo sapiens (human) / References: UniProt: O75718 |
#3: Protein | Mass: 28669.605 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: PPIB, CYPB / Production host: Homo sapiens (human) / References: UniProt: P23284, peptidylprolyl isomerase |
-Protein/peptide / Sugars / Non-polymers , 3 types, 6 molecules E
#4: Protein/peptide | Mass: 1958.185 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) | ||
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#5: Sugar | ChemComp-NAG / #6: Chemical | ChemComp-FE / | |
-Details
Has ligand of interest | Y |
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-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
-Sample preparation
Component | Name: A protein modification complex with synthetic substrate Type: COMPLEX / Entity ID: #1-#4 / Source: RECOMBINANT |
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Source (natural) | Organism: Homo sapiens (human) |
Source (recombinant) | Organism: Homo sapiens (human) |
Buffer solution | pH: 7.5 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Vitrification | Cryogen name: ETHANE |
-Electron microscopy imaging
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
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Microscopy | Model: FEI TITAN KRIOS |
Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: SPOT SCAN |
Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 2600 nm / Nominal defocus min: 1500 nm |
Image recording | Electron dose: 50 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
-Processing
EM software | Name: PHENIX / Version: 1.20.1_4487: / Category: model refinement | ||||||||||||||||||||||||
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
3D reconstruction | Resolution: 3.18 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 1779834 / Symmetry type: POINT | ||||||||||||||||||||||||
Refine LS restraints |
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