Utilization of Ketone Bodies / cellular ketone body metabolic process / 3-oxoacid CoA-transferase / succinyl-CoA:3-oxo-acid CoA-transferase activity / ketone body catabolic process / Mitochondrial protein degradation / protein homodimerization activity / mitochondrion Similarity search - Function
3-oxoacid CoA-transferase, subunit A / Coenzyme A transferase active site / 3-oxoacid CoA-transferase / Coenzyme A transferases signature 2. / Coenzyme A transferase binding site / 3-oxoacid CoA-transferase, subunit B / Coenzyme A transferases signature 1. / Glutaconate Coenzyme A-transferase / Glutaconate Coenzyme A-transferase / Coenzyme A transferase family I ...3-oxoacid CoA-transferase, subunit A / Coenzyme A transferase active site / 3-oxoacid CoA-transferase / Coenzyme A transferases signature 2. / Coenzyme A transferase binding site / 3-oxoacid CoA-transferase, subunit B / Coenzyme A transferases signature 1. / Glutaconate Coenzyme A-transferase / Glutaconate Coenzyme A-transferase / Coenzyme A transferase family I / Coenzyme A transferase / Coenzyme A transferase / NagB/RpiA transferase-like / 3-Layer(aba) Sandwich / Alpha Beta Similarity search - Domain/homology
ETHYL MERCURY ION / 2-(ETHYLMERCURI-THIO)-BENZOIC ACID / Succinyl-CoA:3-ketoacid coenzyme A transferase 1, mitochondrial Similarity search - Component
Biological species
SUS SCROFA (pig)
Method
X-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 2.4 Å
SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED.
A: SUCCINYL-COA\:3-KETOACID-COENZYME A TRANSFERASE B: SUCCINYL-COA\:3-KETOACID-COENZYME A TRANSFERASE C: SUCCINYL-COA\:3-KETOACID-COENZYME A TRANSFERASE D: SUCCINYL-COA\:3-KETOACID-COENZYME A TRANSFERASE hetero molecules
Mass: 18.015 Da / Num. of mol.: 512 / Source method: isolated from a natural source / Formula: H2O
Compound details
KEY ENZYME FOR KETONE BODY CATABOLISM. TRANSFERS THE COA MOIETY FROM SUCCINATE TO ACETOACETATE. ...KEY ENZYME FOR KETONE BODY CATABOLISM. TRANSFERS THE COA MOIETY FROM SUCCINATE TO ACETOACETATE. FORMATION OF THE ENZYME-COA INTERMEDIATE PROCEEDS VIA AN UNSTABLE ANHYDRIDE SPECIES FORMED BETWEEN THE CARBOXYLATE GROUPS OF THE ENZYME AND SUBSTRATE.
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Experimental details
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Experiment
Experiment
Method: X-RAY DIFFRACTION / Number of used crystals: 1
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Sample preparation
Crystal
Density Matthews: 2.36 Å3/Da / Density % sol: 47.91 %
Monochromator: SI / Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength
ID
Wavelength (Å)
Relative weight
1
1.008
1
2
0.83
1
Reflection
Resolution: 2.4→30 Å / Num. obs: 73890 / % possible obs: 94.8 % / Redundancy: 3.7 % / Biso Wilson estimate: 39.6 Å2 / Rsym value: 0.052 / Net I/σ(I): 10
Reflection shell
Resolution: 2.4→2.53 Å / Redundancy: 3.6 % / Mean I/σ(I) obs: 2.8 / Rsym value: 0.27 / % possible all: 99.8
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Processing
Software
Name
Version
Classification
CNS
1
refinement
DENZO
datareduction
SCALA
datascaling
Refinement
Method to determine structure: MAD / Resolution: 2.4→29.76 Å / Rfactor Rfree error: 0.007 / Data cutoff high absF: 2143399.14 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 Details: RESIDUES IN THE SERVERAL REGIONS WERE NOT VISIBLE IN ELECTRON DENSITY MAPS AND WERE NOT MODELLED: A/B287-299,C286-299, D283-299, B/C401-419, B/C441-465
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