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- EMDB-20525: ChsH1-ChsH2-Ltp2 complex -

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Basic information

Entry
Database: EMDB / ID: EMD-20525
TitleChsH1-ChsH2-Ltp2 complex
Map data
Samplean enoyl-CoA hydratase retro-aldolase complex
Biological speciesMycobacterium tuberculosis (bacteria)
Methodsingle particle reconstruction / Resolution: 24 Å
AuthorsYang M / Yuan T / Gehring K / Sampson N
Funding support United States, 1 items
OrganizationGrant numberCountry
National Institutes of Health/National Human Genome Research InstituteRO1AI134054 United States
CitationJournal: 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
DepositionJul 30, 2019-
Header (metadata) releaseOct 9, 2019-
Map releaseOct 9, 2019-
UpdateOct 9, 2019-
Current statusOct 9, 2019Processing site: RCSB / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.06
  • Imaged by UCSF Chimera
  • Download
  • Surface view colored by radius
  • Surface level: 0.06
  • Imaged by UCSF Chimera
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

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Map

FileDownload / File: emd_20525.map.gz / Format: CCP4 / Size: 30.5 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.8 Å/pix.
x 200 pix.
= 360. Å
1.8 Å/pix.
x 200 pix.
= 360. Å
1.8 Å/pix.
x 200 pix.
= 360. Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.8 Å
Density
Contour LevelBy AUTHOR: 0.06 / Movie #1: 0.06
Minimum - Maximum-0.019052302 - 0.12076074
Average (Standard dev.)0.0011870575 (±0.0095204525)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions200200200
Spacing200200200
CellA=B=C: 360.0 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.81.81.8
M x/y/z200200200
origin x/y/z0.0000.0000.000
length x/y/z360.000360.000360.000
α/β/γ90.00090.00090.000
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS200200200
D min/max/mean-0.0190.1210.001

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Supplemental data

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Sample components

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Entire an enoyl-CoA hydratase retro-aldolase complex

EntireName: an enoyl-CoA hydratase retro-aldolase complex / Number of components: 1

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Component #1: protein, an enoyl-CoA hydratase retro-aldolase complex

ProteinName: an enoyl-CoA hydratase retro-aldolase complex / Recombinant expression: No
MassExperimental: 180 kDa
SourceSpecies: Mycobacterium tuberculosis (bacteria)
Source (engineered)Expression System: Rhodococcus jostii RHA1 (bacteria)

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Experimental details

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Sample preparation

SpecimenSpecimen state: Particle
Sample solutionpH: 8
VitrificationCryogen name: NONE

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Electron microscopy imaging

Experimental equipment
Model: Tecnai F20 / Image courtesy: FEI Company
ImagingMicroscope: FEI TECNAI F20
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 200 kV / Electron dose: 30 e/Å2 / Illumination mode: SPOT SCAN
LensImaging mode: BRIGHT FIELD
Specimen HolderModel: OTHER
CameraDetector: GATAN MULTISCAN

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Image processing

ProcessingMethod: single particle reconstruction / Applied symmetry: C2 (2 fold cyclic) / Number of projections: 36899
3D reconstructionResolution: 24 Å / Resolution method: FSC 0.143 CUT-OFF
FSC plot (resolution estimation)

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