|Entry||Database: EMDB / ID: EMD-20525|
|Sample||an enoyl-CoA hydratase retro-aldolase complex|
|Biological species||Mycobacterium tuberculosis (bacteria)|
|Method||single particle reconstruction / negative staining / Resolution: 24 Å|
|Authors||Yang M / Yuan T / Gehring K / Sampson N|
|Funding support|| United States, 1 items |
|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 .
|Structure viewer||EM map: |
Downloads & links
|File||Download / File: emd_20525.map.gz / Format: CCP4 / Size: 30.5 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)|
|Projections & slices|
Images are generated by Spider.
|Voxel size||X=Y=Z: 1.8 Å|
|Symmetry||Space group: 1|
CCP4 map header:
-Half map: half map 2
|Annotation||half map 2|
|Projections & Slices|
-Half map: Half map 1
-Entire an enoyl-CoA hydratase retro-aldolase complex
|Entire||Name: an enoyl-CoA hydratase retro-aldolase complex / Number of components: 1|
-Component #1: protein, an enoyl-CoA hydratase retro-aldolase complex
|Protein||Name: an enoyl-CoA hydratase retro-aldolase complex / Recombinant expression: No|
|Mass||Experimental: 180 kDa|
|Source||Species: Mycobacterium tuberculosis (bacteria)|
|Source (engineered)||Expression System: Rhodococcus jostii RHA1 (bacteria)|
|Specimen||Specimen state: Particle / Method: negative staining|
|Sample solution||pH: 8|
|Vitrification||Cryogen name: NONE|
-Electron microscopy imaging
Model: Tecnai F20 / Image courtesy: FEI Company
|Imaging||Microscope: FEI TECNAI F20|
|Electron gun||Electron source: FIELD EMISSION GUN / Accelerating voltage: 200 kV / Electron dose: 30 e/Å2 / Illumination mode: SPOT SCAN|
|Lens||Imaging mode: BRIGHT FIELD|
|Specimen Holder||Model: OTHER|
|Camera||Detector: GATAN MULTISCAN|
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