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- PDB-6b0u: Crystal structure of acetyltransferase Eis from Mycobacterium tub... -
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Open data
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Basic information
Entry | Database: PDB / ID: 6b0u | ||||||
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Title | Crystal structure of acetyltransferase Eis from Mycobacterium tuberculosis in complex with a Lys-containing peptide | ||||||
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![]() | TRANSFERASE / histone acetylation / aminoglycoside / drug resistance / tuberculosis / acetylation | ||||||
Function / homology | ![]() effector-mediated defense to host-produced reactive oxygen species / symbiont-mediated perturbation of host inflammatory response / symbiont-mediated suppression of host defense-related programmed cell death / aminoglycoside antibiotic catabolic process / aminoglycoside N-acetyltransferase activity / symbiont-mediated perturbation of host innate immune response / Suppression of autophagy / symbiont-mediated perturbation of host programmed cell death / bacterial extracellular vesicle / biological process involved in interaction with host ...effector-mediated defense to host-produced reactive oxygen species / symbiont-mediated perturbation of host inflammatory response / symbiont-mediated suppression of host defense-related programmed cell death / aminoglycoside antibiotic catabolic process / aminoglycoside N-acetyltransferase activity / symbiont-mediated perturbation of host innate immune response / Suppression of autophagy / symbiont-mediated perturbation of host programmed cell death / bacterial extracellular vesicle / biological process involved in interaction with host / host cell cytoplasmic vesicle / N-acetyltransferase activity / peptide-lysine-N-acetyltransferase activity / Transferases; Acyltransferases; Transferring groups other than aminoacyl groups / host extracellular space / response to antibiotic / identical protein binding / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Biswas, T. / Pang, A.H. / Garneau-Tsodikova, S. / Tsodikov, O.V. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Acetylation by Eis and Deacetylation by Rv1151c of Mycobacterium tuberculosis HupB: Biochemical and Structural Insight. Authors: Green, K.D. / Biswas, T. / Pang, A.H. / Willby, M.J. / Reed, M.S. / Stuchlik, O. / Pohl, J. / Posey, J.E. / Tsodikov, O.V. / Garneau-Tsodikova, S. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 238.8 KB | Display | ![]() |
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PDB format | ![]() | 190.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 3r1kS S: Starting model for refinement |
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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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Unit cell |
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Components
#1: Protein | Mass: 46692.902 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Strain: ATCC 25618 / H37Rv / Gene: eis, Rv2416c, MTCY253.04 / Production host: ![]() ![]() References: UniProt: P9WFK7, Transferases; Acyltransferases; Transferring groups other than aminoacyl groups #2: Protein/peptide | Mass: 888.084 Da / Num. of mol.: 2 / Source method: obtained synthetically Source: (synth.) ![]() #3: Chemical | ChemComp-COA / |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.5 Å3/Da / Density % sol: 50.78 % |
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Crystal grow | Temperature: 295 K / Method: vapor diffusion, hanging drop / pH: 8.5 Details: peptide (1 mM) and CoA (1 mM) with protein in a 1:1 ration with reservoir solution (Tris-HCl (100 mM, pH 8.5) and PEG 8,000 (13% w/v)) |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Oct 4, 2012 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97 Å / Relative weight: 1 |
Reflection | Resolution: 2.8→37.71 Å / Num. obs: 30053 / % possible obs: 87 % / Observed criterion σ(I): 2.8 / Redundancy: 2.9 % / Rmerge(I) obs: 0.06 / Net I/σ(I): 14 |
Reflection shell | Resolution: 2.8→2.85 Å / Rmerge(I) obs: 0.24 / % possible all: 87 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 3R1K Resolution: 2.8→37 Å / Cor.coef. Fo:Fc: 0.934 / Cor.coef. Fo:Fc free: 0.891 / SU B: 20.379 / SU ML: 0.364 / Cross valid method: THROUGHOUT / ESU R Free: 0.442 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 59.785 Å2
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Refinement step | Cycle: 1 / Resolution: 2.8→37 Å
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Refine LS restraints |
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