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Yorodumi- PDB-4y49: Crystal structure of yeast N-terminal acetyltransferase (ppGpp) N... -
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-Basic information
Entry | Database: PDB / ID: 4y49 | ||||||
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Title | Crystal structure of yeast N-terminal acetyltransferase (ppGpp) NatE in complex with a bisubstrate | ||||||
Components |
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Keywords | TRANSFERASE / N-terminal acetyltransferase / NatE / ppGpp / bisubstrate | ||||||
Function / homology | Function and homology information cellular pigmentation / positive regulation of oxytocin production / Peptide hormone biosynthesis / Defective ACTH causes obesity and POMCD / type 1 melanocortin receptor binding / N-terminal protein amino acid propionylation / type 3 melanocortin receptor binding / type 4 melanocortin receptor binding / regulation of corticosterone secretion / peptide-glutamate-alpha-N-acetyltransferase activity ...cellular pigmentation / positive regulation of oxytocin production / Peptide hormone biosynthesis / Defective ACTH causes obesity and POMCD / type 1 melanocortin receptor binding / N-terminal protein amino acid propionylation / type 3 melanocortin receptor binding / type 4 melanocortin receptor binding / regulation of corticosterone secretion / peptide-glutamate-alpha-N-acetyltransferase activity / response to melanocyte-stimulating hormone / Opioid Signalling / N-terminal amino-acid Nalpha-acetyltransferase NatA / N-terminal methionine Nalpha-acetyltransferase NatE / peptide-serine-alpha-N-acetyltransferase activity / NatA complex / Androgen biosynthesis / regulation of appetite / N-terminal protein amino acid acetylation / peptide alpha-N-acetyltransferase activity / regulation of glycogen metabolic process / Glucocorticoid biosynthesis / mitotic sister chromatid cohesion / negative regulation of tumor necrosis factor production / neuropeptide signaling pathway / Endogenous sterols / FOXO-mediated transcription of oxidative stress, metabolic and neuronal genes / positive regulation of cAMP-mediated signaling / Peptide ligand-binding receptors / secretory granule / generation of precursor metabolites and energy / G protein-coupled receptor binding / calcium-mediated signaling / G-protein activation / hormone activity / regulation of blood pressure / ribosome binding / glucose homeostasis / cell-cell signaling / G alpha (i) signalling events / G alpha (s) signalling events / Interleukin-4 and Interleukin-13 signaling / secretory granule lumen / signaling receptor binding / signal transduction / positive regulation of transcription by RNA polymerase II / mitochondrion / extracellular space / extracellular region / identical protein binding / cytoplasm Similarity search - Function | ||||||
Biological species | Saccharomyces cerevisiae (brewer's yeast) Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 3.95 Å | ||||||
Authors | Dong, J. / Wang, S. / York, J.D. | ||||||
Citation | Journal: To Be Published Title: Crystal structure of yeast N-terminal acetyltransferase (ppGpp) NatE in complex with a bisubstrate Authors: Dong, J. / Wang, S. / York, J.D. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4y49.cif.gz | 989.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4y49.ent.gz | 760.2 KB | Display | PDB format |
PDBx/mmJSON format | 4y49.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/y4/4y49 ftp://data.pdbj.org/pub/pdb/validation_reports/y4/4y49 | HTTPS FTP |
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-Related structure data
Related structure data | |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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3 |
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Unit cell |
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-Components
-N-terminal acetyltransferase A complex subunit ... , 2 types, 6 molecules AGMCIO
#1: Protein | Mass: 99084.195 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast) Production host: Escherichia coli (E. coli) / References: UniProt: P12945 #3: Protein | Mass: 19753.727 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast) Production host: Escherichia coli (E. coli) References: UniProt: Q08689, Transferases; Acyltransferases; Transferring groups other than aminoacyl groups |
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-Protein / Protein/peptide , 2 types, 6 molecules BHNEKQ
#2: Protein | Mass: 27635.168 Da / Num. of mol.: 3 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast) Production host: Escherichia coli (E. coli) / References: UniProt: P07347, EC: 2.3.1.88 #4: Protein/peptide | Mass: 1058.169 Da / Num. of mol.: 3 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) / References: UniProt: P01189*PLUS |
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-Non-polymers , 3 types, 9 molecules
#5: Chemical | #6: Chemical | #7: Chemical | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.35 Å3/Da / Density % sol: 47.64 % |
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, hanging drop Details: 17% Jeffamine ED-2001 pH 7.0, 0.1 M imidazole, pH 6.2 PH range: 6.2 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 21-ID-G / Wavelength: 0.97856 Å |
Detector | Type: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Jan 30, 2014 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97856 Å / Relative weight: 1 |
Reflection | Resolution: 3.95→49.63 Å / Num. obs: 36307 / % possible obs: 97 % / Redundancy: 6.4 % / Rmerge(I) obs: 0.111 / Net I/σ(I): 8.6 |
Reflection shell | Resolution: 3.95→4.09 Å / Redundancy: 6.8 % / Rmerge(I) obs: 0.343 / Mean I/σ(I) obs: 4.5 / % possible all: 83.9 |
-Processing
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Refinement | Resolution: 3.95→49.63 Å / Cor.coef. Fo:Fc: 0.864 / Cor.coef. Fo:Fc free: 0.839 / SU B: 222.871 / SU ML: 1.31 / Cross valid method: THROUGHOUT / ESU R Free: 1.306 / 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: 84.988 Å2
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Refinement step | Cycle: LAST / Resolution: 3.95→49.63 Å
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