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Yorodumi- PDB-1mja: Crystal structure of yeast Esa1 histone acetyltransferase domain ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1mja | ||||||
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Title | Crystal structure of yeast Esa1 histone acetyltransferase domain complexed with acetyl coenzyme A | ||||||
Components | Esa1 protein | ||||||
Keywords | TRANSFERASE / Esa1 / Histone acetyltransferase / HAT / MYST | ||||||
Function / homology | Function and homology information DNA Damage/Telomere Stress Induced Senescence / Sensing of DNA Double Strand Breaks / piccolo histone acetyltransferase complex / Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks / histone H4K16 acetyltransferase activity / peptide 2-hydroxyisobutyryltransferase activity / histone crotonyltransferase activity / DNA-templated transcription elongation / positive regulation of triglyceride biosynthetic process / histone H4 acetyltransferase activity ...DNA Damage/Telomere Stress Induced Senescence / Sensing of DNA Double Strand Breaks / piccolo histone acetyltransferase complex / Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks / histone H4K16 acetyltransferase activity / peptide 2-hydroxyisobutyryltransferase activity / histone crotonyltransferase activity / DNA-templated transcription elongation / positive regulation of triglyceride biosynthetic process / histone H4 acetyltransferase activity / rDNA heterochromatin formation / peptide N-acetyltransferase activity / NuA4 histone acetyltransferase complex / peptide-lysine-N-acetyltransferase activity / Estrogen-dependent gene expression / positive regulation of macroautophagy / histone acetyltransferase activity / histone acetyltransferase / Transferases; Acyltransferases; Transferring groups other than aminoacyl groups / positive regulation of transcription elongation by RNA polymerase II / transcription coregulator activity / nucleosome / regulation of cell cycle / DNA repair / negative regulation of DNA-templated transcription / DNA-templated transcription / chromatin / regulation of transcription by RNA polymerase II / positive regulation of transcription by RNA polymerase II / nucleus Similarity search - Function | ||||||
Biological species | Saccharomyces cerevisiae (brewer's yeast) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.26 Å | ||||||
Authors | Yan, Y. / Harper, S. / Speicher, D. / Marmorstein, R. | ||||||
Citation | Journal: Nat.Struct.Biol. / Year: 2002 Title: The catalytic mechanism of the ESA1 histone acetyltransferase involves a self-acetylated intermediate. Authors: Yan, Y. / Harper, S. / Speicher, D.W. / Marmorstein, R. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1mja.cif.gz | 70.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1mja.ent.gz | 57.2 KB | Display | PDB format |
PDBx/mmJSON format | 1mja.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/mj/1mja ftp://data.pdbj.org/pub/pdb/validation_reports/mj/1mja | HTTPS FTP |
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-Related structure data
Related structure data | 1mj9C 1mjbC 1fy7S S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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2 |
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3 |
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Unit cell |
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Details | The biological assembly is a monomer, which is also the asymmetric unit. |
-Components
#1: Protein | Mass: 33414.453 Da / Num. of mol.: 1 Fragment: Histone acetyltransferase domain (Residues 160-445) Source method: isolated from a genetically manipulated source Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast) Gene: YOR244W / Plasmid: pRSET-A / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(lysS) / References: UniProt: Q08649 |
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#2: Chemical | ChemComp-COA / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 3.71 Å3/Da / Density % sol: 66.87 % | ||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6.5 Details: sodium cacodylate, ammonium sulfate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 20 ℃ | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 93 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RU200 / Wavelength: 1.5418 Å |
Detector | Type: RIGAKU RAXIS IV / Detector: IMAGE PLATE / Date: Jun 12, 2001 / Details: mirrors |
Radiation | Monochromator: Yale Mirrors / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.26→20 Å / Num. all: 23988 / Num. obs: 23988 / % possible obs: 99.9 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3 / Redundancy: 72.7 % / Rmerge(I) obs: 0.051 / Rsym value: 0.051 / Net I/σ(I): 30.2 |
Reflection shell | Resolution: 2.26→2.34 Å / Redundancy: 9.6 % / Rmerge(I) obs: 0.355 / Mean I/σ(I) obs: 5.9 / Num. unique all: 2338 / Rsym value: 0.355 / % possible all: 99.9 |
Reflection | *PLUS Lowest resolution: 20 Å / Num. obs: 24067 / Num. measured all: 1744021 / Rmerge(I) obs: 0.051 |
Reflection shell | *PLUS Rmerge(I) obs: 0.355 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB entry 1FY7 Resolution: 2.26→20 Å / Isotropic thermal model: Isotropic / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 2.26→20 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.26→2.28 Å /
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Xplor file |
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Refinement | *PLUS Lowest resolution: 20 Å / % reflection Rfree: 10 % / Rfactor Rfree: 0.224 / Rfactor Rwork: 0.212 | |||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Rfactor Rfree: 0.239 / Rfactor Rwork: 0.236 |