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Yorodumi- PDB-9qts: Structure of the energy converting methyltransferase (Mtr) of Met... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 9qts | |||||||||||||||
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| Title | Structure of the energy converting methyltransferase (Mtr) of Methanosarcina mazei in complex with a novel protein binder | |||||||||||||||
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Keywords | MEMBRANE PROTEIN / Sodium-pumping / membrane-bound / methyltransferase complex / methanogen / methanogenic / methylotrophic / archaeon / archaea / methanosarcina / methanosarcina mazei / Vitamin B12 / corrinoid / cobalt / 5-hydroxybenzimidazole / small protein / oxygen-sensitive | |||||||||||||||
| Function / homology | Function and homology informationtetrahydromethanopterin S-methyltransferase / tetrahydromethanopterin S-methyltransferase activity / methanogenesis, from carbon dioxide / vesicle membrane / cobalt ion binding / one-carbon metabolic process / methylation / plasma membrane / cytoplasm Similarity search - Function | |||||||||||||||
| Biological species | Methanosarcina mazei Go1 (archaea) | |||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.1 Å | |||||||||||||||
Authors | Reif-Trauttmansdorff, T. / Herdering, E. / Bohn, S. / Pascoa, T.C. / Kumar, A. / Zimmer, E. / Schmitz, R.A. / Schuller, J.M. | |||||||||||||||
| Funding support | European Union, 1items
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Citation | Journal: Nat Commun / Year: 2025Title: Structure of the Methanosarcina mazei Mtr complex bound to the oxygen-stress responsive small protein MtrI Authors: Reif-Trauttmansdorff, T. / Herdering, E. / Bohn, S. / Pascoa, T.C. / Kumar, A. / Zimmer, E. / Schmitz, R.A. / Schuller, J.M. | |||||||||||||||
| History |
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 9qts.cif.gz | 1.4 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb9qts.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 9qts.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/qt/9qts ftp://data.pdbj.org/pub/pdb/validation_reports/qt/9qts | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 53361MC ![]() 9qtpC ![]() 9qtqC ![]() 9qtrC C: citing same article ( M: map data used to model this data |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
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Assembly
| Deposited unit | ![]()
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Components
-Tetrahydromethanopterin S-methyltransferase subunit ... , 8 types, 27 molecules ABCDEFGHIJKLMNOPQRSTUmnopqr
| #1: Protein | Mass: 25395.191 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Methanosarcina mazei Go1 (archaea) / Gene: mtrA, MM_1543 / Production host: Methanosarcina mazei Go1 (archaea)References: UniProt: O59640, tetrahydromethanopterin S-methyltransferase #2: Protein | Mass: 11879.630 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Methanosarcina mazei Go1 (archaea) / Gene: mtrB, MM_1544 / Production host: Methanosarcina mazei Go1 (archaea)References: UniProt: P80655, tetrahydromethanopterin S-methyltransferase #3: Protein | Mass: 26953.893 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Methanosarcina mazei Go1 (archaea) / Gene: mtrC, MM_1545 / Production host: Methanosarcina mazei Go1 (archaea)References: UniProt: O59638, tetrahydromethanopterin S-methyltransferase #4: Protein | Mass: 25279.777 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Methanosarcina mazei Go1 (archaea) / Gene: mtrD, MM_1546 / Production host: Methanosarcina mazei Go1 (archaea)References: UniProt: P80653, tetrahydromethanopterin S-methyltransferase #5: Protein | Mass: 35539.625 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Details: c-terminal Twin-StrepTag / Source: (gene. exp.) Methanosarcina mazei Go1 (archaea) / Gene: mtrE, MM_1547 / Production host: Methanosarcina mazei Go1 (archaea)References: UniProt: P80651, tetrahydromethanopterin S-methyltransferase #6: Protein | Mass: 7573.959 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Methanosarcina mazei Go1 (archaea) / Gene: mtrF, MM_1542 / Production host: Methanosarcina mazei Go1 (archaea)References: UniProt: P80654, tetrahydromethanopterin S-methyltransferase #7: Protein | Mass: 8030.405 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Methanosarcina mazei Go1 (archaea) / Gene: mtrG, MM_1541 / Production host: Methanosarcina mazei Go1 (archaea)References: UniProt: P80656, tetrahydromethanopterin S-methyltransferase #9: Protein | Mass: 34075.730 Da / Num. of mol.: 6 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Methanosarcina mazei Go1 (archaea) / Gene: mtrH, MM_1540 / Production host: Methanosarcina mazei Go1 (archaea)References: UniProt: P80650, tetrahydromethanopterin S-methyltransferase |
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-Protein , 1 types, 1 molecules i
| #8: Protein | Mass: 7623.597 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Methanosarcina mazei Go1 (archaea) / Gene: MM_2401 / Production host: Methanosarcina mazei Go1 (archaea) / References: UniProt: Q8PUD4 |
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-Non-polymers , 7 types, 2660 molecules 






| #10: Chemical | ChemComp-B13 / | ||||||||||
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| #11: Chemical | ChemComp-A1JAP / Mass: 836.214 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C46H94NO9P / Feature type: SUBJECT OF INVESTIGATION #12: Chemical | #13: Chemical | Mass: 911.277 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C49H99O12P / Feature type: SUBJECT OF INVESTIGATION #14: Chemical | #15: Chemical | Mass: 776.205 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C45H94NO6P / Feature type: SUBJECT OF INVESTIGATION #16: Water | ChemComp-HOH / | |
-Details
| Has ligand of interest | Y |
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| Has protein modification | N |
-Experimental details
-Experiment
| Experiment | Method: ELECTRON MICROSCOPY |
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| EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
| Component | Name: Mtr complex / Type: COMPLEX / Entity ID: #1-#9 / Source: NATURAL |
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| Molecular weight | Experimental value: NO |
| Source (natural) | Organism: Methanosarcina mazei Go1 (archaea) |
| Buffer solution | pH: 7 |
| Specimen | Conc.: 10 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Vitrification | Cryogen name: ETHANE-PROPANE |
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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| Microscopy | Model: TFS KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 3500 nm / Nominal defocus min: 500 nm |
| Image recording | Electron dose: 60 e/Å2 / Film or detector model: FEI FALCON IV (4k x 4k) |
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Processing
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| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
| 3D reconstruction | Resolution: 2.1 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 150000 / Symmetry type: POINT | ||||||||||||||||||||||||
| Refinement | Cross valid method: NONE Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2 | ||||||||||||||||||||||||
| Displacement parameters | Biso mean: 44.06 Å2 | ||||||||||||||||||||||||
| Refine LS restraints |
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Methanosarcina mazei Go1 (archaea)
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FIELD EMISSION GUN