[English] 日本語
Yorodumi- PDB-1z60: Solution structure of the carboxy-terminal domain of human TFIIH ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1z60 | |||||||||
---|---|---|---|---|---|---|---|---|---|---|
Title | Solution structure of the carboxy-terminal domain of human TFIIH P44 subunit | |||||||||
Components | TFIIH basal transcription factor complex p44 subunit | |||||||||
Keywords | TRANSCRIPTION / Basic transcription factor / zinc binding protein / ring finger | |||||||||
Function / homology | Function and homology information core TFIIH complex portion of holo TFIIH complex / G protein-coupled receptor internalization / transcription factor TFIIH core complex / transcription factor TFIIH holo complex / RNA Polymerase I Transcription Termination / RNA Pol II CTD phosphorylation and interaction with CE during HIV infection / RNA Pol II CTD phosphorylation and interaction with CE / Formation of the Early Elongation Complex / Formation of the HIV-1 Early Elongation Complex / mRNA Capping ...core TFIIH complex portion of holo TFIIH complex / G protein-coupled receptor internalization / transcription factor TFIIH core complex / transcription factor TFIIH holo complex / RNA Polymerase I Transcription Termination / RNA Pol II CTD phosphorylation and interaction with CE during HIV infection / RNA Pol II CTD phosphorylation and interaction with CE / Formation of the Early Elongation Complex / Formation of the HIV-1 Early Elongation Complex / mRNA Capping / HIV Transcription Initiation / RNA Polymerase II HIV Promoter Escape / Transcription of the HIV genome / RNA Polymerase II Promoter Escape / RNA Polymerase II Transcription Pre-Initiation And Promoter Opening / RNA Polymerase II Transcription Initiation / RNA Polymerase II Transcription Initiation And Promoter Clearance / RNA Polymerase I Transcription Initiation / transcription factor TFIID complex / RNA polymerase II general transcription initiation factor activity / Tat-mediated elongation of the HIV-1 transcript / Formation of HIV-1 elongation complex containing HIV-1 Tat / Formation of HIV elongation complex in the absence of HIV Tat / RNA Polymerase II Transcription Elongation / Formation of RNA Pol II elongation complex / response to UV / RNA Polymerase II Pre-transcription Events / nucleotide-excision repair / RNA Polymerase I Promoter Escape / TP53 Regulates Transcription of DNA Repair Genes / transcription initiation at RNA polymerase II promoter / NoRC negatively regulates rRNA expression / Dual Incision in GG-NER / Transcription-Coupled Nucleotide Excision Repair (TC-NER) / Formation of TC-NER Pre-Incision Complex / Formation of Incision Complex in GG-NER / Dual incision in TC-NER / Gap-filling DNA repair synthesis and ligation in TC-NER / transcription by RNA polymerase II / nuclear speck / regulation of transcription by RNA polymerase II / zinc ion binding / nucleoplasm / nucleus Similarity search - Function | |||||||||
Biological species | Homo sapiens (human) | |||||||||
Method | SOLUTION NMR / simulated annealing | |||||||||
Authors | Kellenberger, E. / Dominguez, C. / Fribourg, S. / Wasielewski, E. / Moras, D. / Poterszman, A. / Boelens, R. / Kieffer, B. | |||||||||
Citation | Journal: J.Biol.Chem. / Year: 2005 Title: Solution structure of the C-terminal domain of TFIIH P44 subunit reveals a novel type of C4C4 ring domain involved in protein-protein interactions. Authors: Kellenberger, E. / Dominguez, C. / Fribourg, S. / Wasielewski, E. / Moras, D. / Poterszman, A. / Boelens, R. / Kieffer, B. #1: Journal: J.Biol.Chem. / Year: 2000 Title: Structural characterization of the cysteine-rich domain of TFIIH p44 subunit Authors: Fribourg, S. / Kellenberger, E. / Rogniaux, H. / Poterszman, A. / Van Dorsselaer, A. / Thierry, J.C. / Egly, J.M. / Moras, D. / Kieffer, B. | |||||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 1z60.cif.gz | 180.6 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb1z60.ent.gz | 146.8 KB | Display | PDB format |
PDBx/mmJSON format | 1z60.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1z60_validation.pdf.gz | 357.3 KB | Display | wwPDB validaton report |
---|---|---|---|---|
Full document | 1z60_full_validation.pdf.gz | 441.3 KB | Display | |
Data in XML | 1z60_validation.xml.gz | 16.8 KB | Display | |
Data in CIF | 1z60_validation.cif.gz | 26 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/z6/1z60 ftp://data.pdbj.org/pub/pdb/validation_reports/z6/1z60 | HTTPS FTP |
-Related structure data
Similar structure data |
---|
-Links
-Assembly
Deposited unit |
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR ensembles |
|
-Components
#1: Protein | Mass: 6695.528 Da / Num. of mol.: 1 / Fragment: C-TERMINAL DOMAIN / Mutation: C381S Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Plasmid: PGEX / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: Q13888 |
---|---|
#2: Chemical |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
NMR experiment |
| ||||||||||||||||||||
NMR details | Text: 113Cd-1H HSQC spectrum was recorded using a broadband z-gradient probe at 293 K |
-Sample preparation
Details |
| ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Sample conditions |
|
-NMR measurement
NMR spectrometer | Type: Bruker DRX / Manufacturer: Bruker / Model: DRX / Field strength: 600 MHz |
---|
-Processing
NMR software |
| ||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method: simulated annealing / Software ordinal: 1 Details: Automated assignment of the NOE was performed, The structures are based on 1294 unambiguous NOE-derived distance constraints, 32 dihedral angle restraints and 17 distance restraints from ...Details: Automated assignment of the NOE was performed, The structures are based on 1294 unambiguous NOE-derived distance constraints, 32 dihedral angle restraints and 17 distance restraints from hydrogen bonds. Geometry of the zinc binding site II is distorded due to conformational exchange averaging. | ||||||||||||||||||||
NMR representative | Selection criteria: the best geometry | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 50 / Conformers submitted total number: 10 |