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Open data
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Basic information
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| Title | cryo-EM map of encapsulin Mmp1 with SufS | |||||||||||||||
Map data | holo-Mmp1 | |||||||||||||||
Sample |
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Keywords | Complex / Mmp1 encapasulin / SufS / STRUCTURAL PROTEIN | |||||||||||||||
| Biological species | Mycolicibacterium smegmatis (bacteria) | |||||||||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.08 Å | |||||||||||||||
Authors | Zhang M / Tang Y / Gao Y / Liu X / Lan W / Liu Y / Ma M | |||||||||||||||
| Funding support | China, 4 items
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Citation | Journal: Commun Biol / Year: 2024Title: The structural and functional analysis of mycobacteria cysteine desulfurase-loaded encapsulin. Authors: Yanting Tang / Yanyan Liu / Mingjing Zhang / Weiqi Lan / Mengyuan Ma / Cheng Chen / Saibin Wu / Rong Chen / Yiran Yan / Lu Feng / Ying Li / Luke W Guddat / Yan Gao / Xiang Liu / Zihe Rao / ![]() Abstract: Encapsulin nanocompartments loaded with dedicated cargo proteins via unique targeting peptides, play a key role in stress resistance, iron storage and natural product biosynthesis. Mmp1 and cysteine ...Encapsulin nanocompartments loaded with dedicated cargo proteins via unique targeting peptides, play a key role in stress resistance, iron storage and natural product biosynthesis. Mmp1 and cysteine desulfurase (Enc-CD) have been identified as the most abundant representatives of family 2 encapsulin systems. However, the molecular assembly, catalytic mechanism, and physiological functions of the Mmp1 encapsulin system have not been studied in detail. Here we isolate and characterize an Enc-CD-loaded Mmp1 encapsulin system from Mycobacterium smegmatis mc155. The cryo-EM structure of the Mmp1 encapsulin and the crystal structure of the naked cargo Enc-CD have been determined. The structure shows that the Mmp1 protomer assembles two conformation models, the icosahedron (T = 1) and homodecamer, with the resolution of 2.60 Å and 2.69 Å. The Enc-CD at 2.10 Å resolution is dimeric and loaded into the Mmp1 (T = 1) encapsulin through the N-terminal long disordered region. Mmp1 encapsulin protects Enc-CD against oxidation as well as to maintain structural stability. These studies provide new insights into the mechanism by which Enc-CD-loaded encapsulin stores sulfur and provides a framework for discovery of new anti-mycobacterial therapeutics. | |||||||||||||||
| History |
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Structure visualization
| Supplemental images |
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Downloads & links
-EMDB archive
| Map data | emd_60569.map.gz | 118.2 MB | EMDB map data format | |
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| Header (meta data) | emd-60569-v30.xml emd-60569.xml | 12.8 KB 12.8 KB | Display Display | EMDB header |
| Images | emd_60569.png | 58.8 KB | ||
| Filedesc metadata | emd-60569.cif.gz | 3.9 KB | ||
| Others | emd_60569_half_map_1.map.gz emd_60569_half_map_2.map.gz | 116.3 MB 116.3 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-60569 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-60569 | HTTPS FTP |
-Validation report
| Summary document | emd_60569_validation.pdf.gz | 1.2 MB | Display | EMDB validaton report |
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| Full document | emd_60569_full_validation.pdf.gz | 1.2 MB | Display | |
| Data in XML | emd_60569_validation.xml.gz | 14.1 KB | Display | |
| Data in CIF | emd_60569_validation.cif.gz | 16.6 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-60569 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-60569 | HTTPS FTP |
-Related structure data
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Links
| EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Map
| File | Download / File: emd_60569.map.gz / Format: CCP4 / Size: 125 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Annotation | holo-Mmp1 | ||||||||||||||||||||||||||||||||||||
| Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 1.06 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Half map: holo-Mmp1
| File | emd_60569_half_map_1.map | ||||||||||||
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| Annotation | holo-Mmp1 | ||||||||||||
| Projections & Slices |
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| Density Histograms |
-Half map: holo-Mmp1
| File | emd_60569_half_map_2.map | ||||||||||||
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| Annotation | holo-Mmp1 | ||||||||||||
| Projections & Slices |
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| Density Histograms |
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Sample components
-Entire : cryo-EM map of encapsulin Mmp1 with SufS
| Entire | Name: cryo-EM map of encapsulin Mmp1 with SufS |
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| Components |
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-Supramolecule #1: cryo-EM map of encapsulin Mmp1 with SufS
| Supramolecule | Name: cryo-EM map of encapsulin Mmp1 with SufS / type: complex / ID: 1 / Parent: 0 |
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| Source (natural) | Organism: Mycolicibacterium smegmatis (bacteria) |
-Experimental details
-Structure determination
| Method | cryo EM |
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Processing | single particle reconstruction |
| Aggregation state | particle |
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Sample preparation
| Buffer | pH: 7.4 |
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| Vitrification | Cryogen name: ETHANE |
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Electron microscopy
| Microscope | FEI TITAN KRIOS |
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| Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 50.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 1.8 µm / Nominal defocus min: 1.2 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
| Startup model | Type of model: NONE |
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| Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 3.08 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 139110 |
| Initial angle assignment | Type: MAXIMUM LIKELIHOOD |
| Final angle assignment | Type: MAXIMUM LIKELIHOOD |
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About Yorodumi




Keywords
Mycolicibacterium smegmatis (bacteria)
Authors
China, 4 items
Citation




Z (Sec.)
Y (Row.)
X (Col.)




































FIELD EMISSION GUN
