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- PDB-6zzi: Crystal structure of the catalyic domain of Corynebacterium gluta... -
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Open data
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Basic information
Entry | Database: PDB / ID: 6zzi | ||||||
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Title | Crystal structure of the catalyic domain of Corynebacterium glutamicum acetyltransferase AceF (E2p). | ||||||
![]() | Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex | ||||||
![]() | TRANSFERASE / PDH / ODH / acetyltransferase / lipoamide / corynebacterium / CoA | ||||||
Function / homology | ![]() dihydrolipoyllysine-residue succinyltransferase activity / dihydrolipoyllysine-residue acetyltransferase / dihydrolipoyllysine-residue acetyltransferase activity / tricarboxylic acid cycle / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Bruch, E.M. / Lexa-Sapart, N. / Bellinzoni, M. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Actinobacteria challenge the paradigm: A unique protein architecture for a well-known, central metabolic complex. Authors: Eduardo M Bruch / Pierre Vilela / Lu Yang / Alexandra Boyko / Norik Lexa-Sapart / Bertrand Raynal / Pedro M Alzari / Marco Bellinzoni / ![]() ![]() Abstract: α-oxoacid dehydrogenase complexes are large, tripartite enzymatic machineries carrying out key reactions in central metabolism. Extremely conserved across the tree of life, they have been, so far, ...α-oxoacid dehydrogenase complexes are large, tripartite enzymatic machineries carrying out key reactions in central metabolism. Extremely conserved across the tree of life, they have been, so far, all considered to be structured around a high-molecular weight hollow core, consisting of up to 60 subunits of the acyltransferase component. We provide here evidence that Actinobacteria break the rule by possessing an acetyltranferase component reduced to its minimally active, trimeric unit, characterized by a unique C-terminal helix bearing an actinobacterial specific insertion that precludes larger protein oligomerization. This particular feature, together with the presence of an gene coding for both the decarboxylase and the acyltransferase domains on the same polypetide, is spread over Actinobacteria and reflects the association of PDH and ODH into a single physical complex. Considering the central role of the pyruvate and 2-oxoglutarate nodes in central metabolism, our findings pave the way to both therapeutic and metabolic engineering applications. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 565.2 KB | Display | ![]() |
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PDB format | ![]() | 469.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 444.6 KB | Display | ![]() |
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Full document | ![]() | 446.4 KB | Display | |
Data in XML | ![]() | 61.1 KB | Display | |
Data in CIF | ![]() | 90.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6zzjC ![]() 6zzkC ![]() 6zzlC ![]() 6zzmC ![]() 6zznC ![]() 4n72S S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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2 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 26161.945 Da / Num. of mol.: 6 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025 Gene: aceF, sucB, Cgl2207, cg2421 / Production host: ![]() ![]() References: UniProt: Q8NNJ2, dihydrolipoyllysine-residue acetyltransferase #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.9 Å3/Da / Density % sol: 57.63 % |
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, sitting drop / Details: 0.1 M Hepes-Na pH 7.5, 5% PEG4000, 30% MPD |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Mar 28, 2015 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9801 Å / Relative weight: 1 |
Reflection | Resolution: 1.932→79.139 Å / Num. obs: 131357 / % possible obs: 99.3 % / Redundancy: 3.8 % / CC1/2: 0.998 / Rpim(I) all: 0.043 / Net I/σ(I): 14 |
Reflection shell | Resolution: 1.932→1.966 Å / Num. unique obs: 6564 / CC1/2: 0.736 / Rpim(I) all: 0.369 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 4N72 Resolution: 1.932→79.14 Å / Cor.coef. Fo:Fc: 0.956 / Cor.coef. Fo:Fc free: 0.947 / SU R Cruickshank DPI: 0.124 / Cross valid method: THROUGHOUT / SU R Blow DPI: 0.128 / SU Rfree Blow DPI: 0.11 / SU Rfree Cruickshank DPI: 0.109
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Displacement parameters | Biso mean: 30.43 Å2
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Refine analyze | Luzzati coordinate error obs: 0.2 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.932→79.14 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.932→1.95 Å
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Refinement TLS params. | Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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