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- PDB-1szd: Structural basis for nicotinamide cleavage and ADP-ribose transfe... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1szd | ||||||
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Title | Structural basis for nicotinamide cleavage and ADP-ribose transfer by NAD+-dependent Sir2 histone/protein deacetylases | ||||||
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![]() | GENE REGULATION / hst2 / Sir2 / Sirtuin / histone deacetylase / protein deacetylase | ||||||
Function / homology | ![]() Transcriptional activation of mitochondrial biogenesis / negative regulation of mitotic recombination / NAD-dependent histone H4K16 deacetylase activity / HATs acetylate histones / RNA polymerase I upstream activating factor complex / Condensation of Prophase Chromosomes / SIRT1 negatively regulates rRNA expression / Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3 / Assembly of the ORC complex at the origin of replication / HDACs deacetylate histones ...Transcriptional activation of mitochondrial biogenesis / negative regulation of mitotic recombination / NAD-dependent histone H4K16 deacetylase activity / HATs acetylate histones / RNA polymerase I upstream activating factor complex / Condensation of Prophase Chromosomes / SIRT1 negatively regulates rRNA expression / Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3 / Assembly of the ORC complex at the origin of replication / HDACs deacetylate histones / rDNA heterochromatin formation / protein acetyllysine N-acetyltransferase / Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks / NAD-dependent histone deacetylase activity / replication fork protection complex / Oxidative Stress Induced Senescence / RMTs methylate histone arginines / SUMOylation of chromatin organization proteins / positive regulation of transcription by RNA polymerase I / RNA Polymerase I Promoter Escape / nucleolar large rRNA transcription by RNA polymerase I / Estrogen-dependent gene expression / NAD+ binding / structural constituent of chromatin / nucleosome / nucleosome assembly / chromatin organization / transferase activity / protein heterodimerization activity / regulation of DNA-templated transcription / DNA binding / nucleus / metal ion binding / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Zhao, K. / Harshaw, R. / Chai, X. / Marmorstein, R. | ||||||
![]() | ![]() Title: Structural basis for nicotinamide cleavage and ADP-ribose transfer by NAD(+)-dependent Sir2 histone/protein deacetylases. Authors: Zhao, K. / Harshaw, R. / Chai, X. / Marmorstein, R. #1: ![]() Title: Structure and Autoregulation Of The Yeast Hst2 Homolog Of Sir2 Authors: Zhao, K. / Harshaw, R. / Chai, X. / Marmorstein, R. #2: ![]() Title: Structure Of The Yeast Hst2 Protein Deacetylase In Ternary Complex With 2'-O-Acetyl ADP Ribose and Histone Peptide Authors: Zhao, K. / Chai, X. / Clements, A. / Marmorstein, R. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 86.8 KB | Display | ![]() |
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PDB format | ![]() | 62.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 764.6 KB | Display | ![]() |
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Full document | ![]() | 774.2 KB | Display | |
Data in XML | ![]() | 18.8 KB | Display | |
Data in CIF | ![]() | 27.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1szcC ![]() 1q1aS C: citing same article ( 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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Unit cell |
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Components
-Protein / Protein/peptide , 2 types, 2 molecules AB
#1: Protein | Mass: 33476.383 Da / Num. of mol.: 1 / Fragment: catalytic core domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Plasmid: hst2 (1-294) / Production host: ![]() ![]() References: UniProt: P53686, Hydrolases; Acting on carbon-nitrogen bonds, other than peptide bonds; In linear amides |
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#2: Protein/peptide | Mass: 1197.457 Da / Num. of mol.: 1 / Source method: obtained synthetically Details: The peptide was chemically synthesized. The sequence of the peptide naturally occurs in Saccharomyces cerevisiae (baker's yeast). References: UniProt: P02309 |
-Non-polymers , 5 types, 346 molecules ![](data/chem/img/CL.gif)
![](data/chem/img/ZN.gif)
![](data/chem/img/APR.gif)
![](data/chem/img/GOL.gif)
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![](data/chem/img/ZN.gif)
![](data/chem/img/APR.gif)
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#3: Chemical | ChemComp-CL / | ||
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#4: Chemical | ChemComp-ZN / | ||
#5: Chemical | ChemComp-APR / | ||
#6: Chemical | #7: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.2 Å3/Da / Density % sol: 61 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion / pH: 6.5 Details: Ammonium Sulfate, Bis-Tris, pH 6.5, VAPOR DIFFUSION, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Aug 8, 2003 |
Radiation | Monochromator: Ni MIRROR + Ni FILTER / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9 Å / Relative weight: 1 |
Reflection | Resolution: 1.5→50 Å / Num. all: 67216 / Num. obs: 67216 / % possible obs: 99 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 1 / Redundancy: 13 % / Biso Wilson estimate: 26.5 Å2 / Rmerge(I) obs: 0.063 / Rsym value: 0.059 / Net I/σ(I): 36.8 |
Reflection shell | Resolution: 1.5→1.55 Å / Redundancy: 3 % / Rmerge(I) obs: 0.484 / Mean I/σ(I) obs: 3.3 / Num. unique all: 6325 / Rsym value: 0.437 / % possible all: 94.3 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1Q1A Resolution: 1.5→28.01 Å / Rfactor Rfree error: 0.005 / Data cutoff high absF: 236729.23 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 60.6629 Å2 / ksol: 0.369871 e/Å3 | ||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 34.4 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 1.5→28.01 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.5→1.59 Å / Rfactor Rfree error: 0.02 / Total num. of bins used: 6
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Xplor file |
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