+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-20525 | |||||||||
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Title | ChsH1-ChsH2-Ltp2 complex | |||||||||
Map data | ChsH1-ChsH2-Ltp2 complex | |||||||||
Sample |
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Keywords | an enoyl-CoA hydratase retro-aldolase complex / cholesterol metabolism / STRUCTURAL PROTEIN | |||||||||
Biological species | Mycobacterium tuberculosis (bacteria) | |||||||||
Method | single particle reconstruction / negative staining / Resolution: 24.0 Å | |||||||||
Authors | Yang M / Yuan T / Gehring K / Sampson N | |||||||||
Funding support | United States, 1 items
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Citation | Journal: Biochemistry / Year: 2019 Title: Exploits a Heterohexameric Enoyl-CoA Hydratase Retro-Aldolase Complex for Cholesterol Catabolism. Authors: Tianao Yuan / Meng Yang / Kalle Gehring / Nicole S Sampson / Abstract: Cholesterol catabolism plays an important role in 's ('s) survival and persistence in the host. exploits three β-oxidation cycles to fully degrade the side chain of cholesterol. Five cistronic ...Cholesterol catabolism plays an important role in 's ('s) survival and persistence in the host. exploits three β-oxidation cycles to fully degrade the side chain of cholesterol. Five cistronic genes in a single operon encode three enzymes, 3-oxo-4-pregnene-20-carboxyl-CoA dehydrogenase (ChsE1-ChsE2), 3-oxo-4,17-pregnadiene-20-carboxyl-CoA hydratase (ChsH1-ChsH2), and 17-hydroxy-3-oxo-4-pregnene-20-carboxyl-CoA retro-aldolase (Ltp2), to perform the last β-oxidation cycle in this pathway. Among these three enzymes, ChsH1-ChsH2 and Ltp2 form a protein complex that is required for the catalysis of carbon-carbon bond cleavage. In this work, we report the structure of the full length ChsH1-ChsH2-Ltp2 complex based on small-angle X-ray scattering and single-particle electron microscopy data. Mutagenesis experiments confirm the requirement for Ltp2 to catalyze the retro-aldol reaction. The structure illustrates how acyl transfer between enzymes may occur. Each protomer of the ChsH1-ChsH2-Ltp2 complex contains three protein components: a chain of ChsH1, a chain of ChsH2, and a chain of Ltp2. Two protomers dimerize at the interface of Ltp2 to form a heterohexameric structure. This unique heterohexameric structure of the ChsH1-ChsH2-Ltp2 complex provides entry to further understand the mechanism of cholesterol catabolism in . | |||||||||
History |
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-Structure visualization
Movie |
Movie viewer |
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Structure viewer | EM map: SurfViewMolmilJmol/JSmol |
Supplemental images |
-Downloads & links
-EMDB archive
Map data | emd_20525.map.gz | 22.3 MB | EMDB map data format | |
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Header (meta data) | emd-20525-v30.xml emd-20525.xml | 11.8 KB 11.8 KB | Display Display | EMDB header |
FSC (resolution estimation) | emd_20525_fsc.xml | 7.2 KB | Display | FSC data file |
Images | emd_20525.png | 16.3 KB | ||
Others | emd_20525_half_map_1.map.gz emd_20525_half_map_2.map.gz | 22.4 MB 22.4 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-20525 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-20525 | HTTPS FTP |
-Validation report
Summary document | emd_20525_validation.pdf.gz | 553.4 KB | Display | EMDB validaton report |
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Full document | emd_20525_full_validation.pdf.gz | 552.9 KB | Display | |
Data in XML | emd_20525_validation.xml.gz | 12.8 KB | Display | |
Data in CIF | emd_20525_validation.cif.gz | 17.5 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-20525 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-20525 | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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-Map
File | Download / File: emd_20525.map.gz / Format: CCP4 / Size: 30.5 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Annotation | ChsH1-ChsH2-Ltp2 complex | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.8 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Half map: half map 2
File | emd_20525_half_map_1.map | ||||||||||||
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Annotation | half map 2 | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: Half map 1
File | emd_20525_half_map_2.map | ||||||||||||
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Annotation | Half map 1 | ||||||||||||
Projections & Slices |
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Density Histograms |
-Sample components
-Entire : an enoyl-CoA hydratase retro-aldolase complex
Entire | Name: an enoyl-CoA hydratase retro-aldolase complex |
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Components |
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-Supramolecule #1: an enoyl-CoA hydratase retro-aldolase complex
Supramolecule | Name: an enoyl-CoA hydratase retro-aldolase complex / type: complex / ID: 1 / Parent: 0 |
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Source (natural) | Organism: Mycobacterium tuberculosis (bacteria) |
Molecular weight | Theoretical: 180 KDa |
-Experimental details
-Structure determination
Method | negative staining |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 8 |
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Staining | Type: NEGATIVE / Material: Uranyl Acetate |
-Electron microscopy
Microscope | FEI TECNAI F20 |
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Image recording | Film or detector model: GATAN MULTISCAN / Average electron dose: 30.0 e/Å2 |
Electron beam | Acceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: SPOT SCAN / Imaging mode: BRIGHT FIELD |
Experimental equipment | Model: Tecnai F20 / Image courtesy: FEI Company |