+Open data
-Basic information
Entry | Database: PDB / ID: 1h89 | ||||||
---|---|---|---|---|---|---|---|
Title | CRYSTAL STRUCTURE OF TERNARY PROTEIN-DNA COMPLEX2 | ||||||
Components |
| ||||||
Keywords | TRANSCRIPTION/DNA / PROTEIN-DNA COMPLEX / TRANSCRIPTION REGULATION / BZIP / PROTO-ONCOGENE / MYB / C-MYB / C/EBP / TRANSCRIPTION-DNA complex | ||||||
Function / homology | Function and homology information C/EBP complex / granuloma formation / regulation of odontoblast differentiation / CHOP-C/EBP complex / positive regulation of sodium-dependent phosphate transport / positive regulation of testosterone secretion / positive regulation of biomineral tissue development / myeloid cell development / positive regulation of hepatic stellate cell proliferation / integrated stress response signaling ...C/EBP complex / granuloma formation / regulation of odontoblast differentiation / CHOP-C/EBP complex / positive regulation of sodium-dependent phosphate transport / positive regulation of testosterone secretion / positive regulation of biomineral tissue development / myeloid cell development / positive regulation of hepatic stellate cell proliferation / integrated stress response signaling / T-helper 1 cell activation / Response of EIF2AK1 (HRI) to heme deficiency / hepatocyte proliferation / positive regulation of hepatic stellate cell activation / positive regulation of transforming growth factor beta production / ATF4 activates genes in response to endoplasmic reticulum stress / regulation of osteoclast differentiation / embryonic digestive tract development / stem cell division / mammary gland epithelial cell differentiation / myeloid cell differentiation / condensed chromosome, centromeric region / regulation of dendritic cell differentiation / cellular response to interleukin-6 / regulation of interleukin-6 production / mammary gland epithelial cell proliferation / WD40-repeat domain binding / histone acetyltransferase binding / positive regulation of interleukin-4 production / regulation of cell differentiation / ubiquitin-like protein ligase binding / Response of EIF2AK4 (GCN2) to amino acid deficiency / Transcriptional Regulation by VENTX / homeostasis of number of cells / intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress / positive regulation of collagen biosynthetic process / embryonic placenta development / positive regulation of fat cell differentiation / RNA polymerase II core promoter sequence-specific DNA binding / Nuclear events stimulated by ALK signaling in cancer / positive regulation of osteoblast differentiation / brown fat cell differentiation / negative regulation of T cell proliferation / ovarian follicle development / positive regulation of glial cell proliferation / spleen development / response to endoplasmic reticulum stress / B cell differentiation / thymus development / cellular response to leukemia inhibitory factor / acute-phase response / liver regeneration / cellular response to amino acid stimulus / RNA polymerase II transcription regulatory region sequence-specific DNA binding / positive regulation of smooth muscle cell proliferation / neuron differentiation / G1/S transition of mitotic cell cycle / chromatin DNA binding / kinase binding / DNA-binding transcription repressor activity, RNA polymerase II-specific / nuclear matrix / histone deacetylase binding / Transcriptional regulation of white adipocyte differentiation / positive regulation of inflammatory response / Transcriptional regulation of granulopoiesis / RNA polymerase II transcription regulator complex / calcium ion transport / positive regulation of neuron apoptotic process / sequence-specific double-stranded DNA binding / positive regulation of cold-induced thermogenesis / mitotic cell cycle / Senescence-Associated Secretory Phenotype (SASP) / regulation of gene expression / DNA-binding transcription activator activity, RNA polymerase II-specific / in utero embryonic development / negative regulation of neuron apoptotic process / response to lipopolysaccharide / transcription by RNA polymerase II / transcription cis-regulatory region binding / DNA-binding transcription factor activity, RNA polymerase II-specific / defense response to bacterium / inflammatory response / immune response / RNA polymerase II cis-regulatory region sequence-specific DNA binding / DNA-binding transcription factor activity / chromatin / regulation of DNA-templated transcription / regulation of transcription by RNA polymerase II / positive regulation of DNA-templated transcription / negative regulation of transcription by RNA polymerase II / protein homodimerization activity / positive regulation of transcription by RNA polymerase II / DNA binding / nucleoplasm / nucleus / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | HOMO SAPIENS (human) MUS MUSCULUS (house mouse) Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.45 Å | ||||||
Authors | Tahirov, T.H. / Ogata, K. | ||||||
Citation | Journal: Cell(Cambridge,Mass.) / Year: 2002 Title: Mechanism of C-Myb-C/Ebpbeta Cooperation from Separated Sites on a Promoter Authors: Tahirov, T.H. / Sato, K. / Ichikawa-Iwata, E. / Sasaki, M. / Inoue-Bungo, T. / Shiina, M. / Kimura, K. / Takata, S. / Fujikawa, A. / Morii, H. / Kumasaka, T. / Yamamoto, M. / Ishii, S. / Ogata, K. #1: Journal: Acta Crystallogr.,Sect.D / Year: 2001 Title: Crystals of Ternary Protein-DNA Complexes Composed of DNA-Binding Domains C-Myb or V-Myb, C/Ebpalpha or C/Ebpbeta and Tom-1A Promoter Fragment Authors: Tahirov, T.H. / Inoue, T. / Sasaki, M. / Shiina, M. / Kimura, K. / Sato, K. / Kumasaka, T. / Yamamoto, M. / Kamiya, N. / Ogata, K. #2: Journal: To be Published Title: Crystal Structures of C-Myb DNA-Binding Domain in Free State: An Evidence for Binding of Na+ and Comparison with Solution Structure Runt Domain, Cbfbeta and the C/Ebpbeta bZIP Region Authors: Tahirov, T.H. / Morii, H. / Uedaira, H. / Sasaki, M. / Sarai, A. / Adachi, S. / Park, S.Y. / Kamiya, N. / Ogata, K. #3: Journal: Cell(Cambridge,Mass.) / Year: 2001 Title: Structural Analyses of DNA Recognition by the Aml1/ Runx-1 Runt Domain and its Allosteric Control by Cbfbeta Authors: Tahirov, T.H. / Inoue-Bungo, T. / Morii, H. / Fujikawa, A. / Sasaki, M. / Kimura, K. / Shiina, M. / Sato, K. / Kumasaka, T. / Yamamoto, M. / Ishii, S. / Ogata, K. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 1h89.cif.gz | 101.1 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb1h89.ent.gz | 72.8 KB | Display | PDB format |
PDBx/mmJSON format | 1h89.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/h8/1h89 ftp://data.pdbj.org/pub/pdb/validation_reports/h8/1h89 | HTTPS FTP |
---|
-Related structure data
Related structure data | 1h88SC 1h8aC S: Starting model for refinement C: citing same article (ref.) |
---|---|
Similar structure data |
-Links
-Assembly
Deposited unit |
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
| ||||||||
Details | OF C/EBP BETA AND MONOMER OF MYB PROTO- ONCOGENE PROTEINBOUND TO A DUPLEX DNA FRAGMENTFOR THE HETERO-ASSEMBLY DESCRIBED BY REMARK 350 THE |
-Components
-Protein , 2 types, 3 molecules ABC
#1: Protein | Mass: 7823.048 Da / Num. of mol.: 2 / Fragment: RESIDUES 273-336 Source method: isolated from a genetically manipulated source Details: BZIP DOMAIN / Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PAR2156 / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P17676 #2: Protein | | Mass: 19173.074 Da / Num. of mol.: 1 / Fragment: RESIDUES 35-193 / Mutation: YES Source method: isolated from a genetically manipulated source Details: DNA BINDING DOMAIN / Source: (gene. exp.) MUS MUSCULUS (house mouse) / Plasmid: PAR2156 / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: GENP: CAA26552, UniProt: P06876*PLUS |
---|
-DNA chain , 2 types, 2 molecules DE
#3: DNA chain | Mass: 8028.177 Da / Num. of mol.: 1 / Fragment: FRAGMENT FROM TOM-1A PROMOTER / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) |
---|---|
#4: DNA chain | Mass: 7948.129 Da / Num. of mol.: 1 / Fragment: FRAGMENT FROM TOM-1A PROMOTER / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) |
-Non-polymers , 2 types, 125 molecules
#5: Chemical | #6: Water | ChemComp-HOH / | |
---|
-Details
Compound details | CHAIN C ENGINEERED MUTATION LYS35MET, ARG36GLY C/EBP BETA IS IMPORTANT TRANSCRIPTIONAL ACTIVATOR IN ...CHAIN C ENGINEERED |
---|---|
Sequence details | LYS 35 WAS REPLACED BY MET AND ARG 36 WAS REPLACED BY GLY BECAUSE OF EXPRESSION |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
---|
-Sample preparation
Crystal | Density Matthews: 3.66 Å3/Da / Density % sol: 65.5 % | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal grow | Temperature: 297 K / Method: vapor diffusion, sitting drop / pH: 7 Details: 0.1 M KCL, 0.05 MGSO4, 4% V/V MPD, 6% V/V GLYCEROL, 0.05 M NA HEPES PH 7.0 AT 24 DEGREES C | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 297 K / pH: 6.8 / Method: vapor diffusion, sitting dropDetails: Tahirov, T.H., (2001) Acta Crystallogr.,Sect.D, 57, 1655. | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
|
-Data collection
Diffraction | Mean temperature: 100 K |
---|---|
Diffraction source | Source: SYNCHROTRON / Site: SPring-8 / Beamline: BL45XU / Wavelength: 1.04 |
Detector | Type: RIGAKU RAXIS IV / Detector: IMAGE PLATE / Date: Nov 17, 1998 / Details: MIRRORS |
Radiation | Monochromator: DIAMOND / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.04 Å / Relative weight: 1 |
Reflection | Resolution: 2.45→20 Å / Num. obs: 27451 / % possible obs: 99 % / Observed criterion σ(I): 0 / Redundancy: 7.496 % / Biso Wilson estimate: 67 Å2 / Rsym value: 0.072 / Net I/σ(I): 27.5043 |
Reflection shell | Resolution: 2.45→2.54 Å / Redundancy: 4 % / Mean I/σ(I) obs: 2.162 / Rsym value: 0.397 / % possible all: 95.5 |
Reflection | *PLUS Highest resolution: 2.45 Å / Lowest resolution: 20 Å / Observed criterion σ(I): 0 / Num. measured all: 205777 / Rmerge(I) obs: 0.072 |
-Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1H88 Resolution: 2.45→19.94 Å / Rfactor Rfree error: 0.007 / Data cutoff high absF: 979672.69 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 Details: BULK SOLVENT MODEL USED. ATOMS C, O, N, CA AND CB ARE HARMONICALLY RESTRAINED DURING REFINEMENT WITH HARMONIC RESTRAINT CONSTANT OF 100
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | Solvent model: FLAT MODEL / Bsol: 38.0889 Å2 / ksol: 0.292803 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 65.6 Å2
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.45→19.94 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell | Resolution: 2.45→2.6 Å / Rfactor Rfree error: 0.027 / Total num. of bins used: 6
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Xplor file |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Software | *PLUS Name: CNS / Version: 0.9 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Lowest resolution: 20 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
|