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- PDB-1zw8: Solution structure of a ZAP1 zinc-responsive domain provides insi... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1zw8 | ||||||
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Title | Solution structure of a ZAP1 zinc-responsive domain provides insights into metalloregulatory transcriptional repression in Saccharomyces cerevisiae | ||||||
![]() | Zinc-responsive transcriptional regulator ZAP1 | ||||||
![]() | TRANSCRIPTION / ZAP1 / interacting C2H2 zinc fingers / beta-beta-alpha / NMR solution structure | ||||||
Function / homology | ![]() cellular response to zinc ion starvation / RNA polymerase II transcription regulatory region sequence-specific DNA binding / DNA-binding transcription factor activity, RNA polymerase II-specific / RNA polymerase II cis-regulatory region sequence-specific DNA binding / regulation of transcription by RNA polymerase II / positive regulation of transcription by RNA polymerase II / zinc ion binding / nucleus Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR / torsion angle dynamics, cartesian refinement | ||||||
![]() | Wang, Z. / Feng, L.S. / Venkataraman, K. / Matskevich, V.A. / Parasuram, P. / Laity, J.H. | ||||||
![]() | ![]() Title: Solution structure of a Zap1 zinc-responsive domain provides insights into metalloregulatory transcriptional repression in Saccharomyces cerevisiae. Authors: Wang, Z. / Feng, L.S. / Matskevich, V. / Venkataraman, K. / Parasuram, P. / Laity, J.H. #1: ![]() Title: Zinc fingers can act as Zn(II) sensors to regulate transcriptional activation domain function Authors: Bird, A.J. / McCal, K. / Kramer, M. / Blankman, E. / Winge, D.R. / Eid, D.J. #2: ![]() Title: Zap1p, a metalloregulatory protein involved in zinc-responsive transcriptional regulation in Saccharomyces cerevisiae Authors: Zhao, H. / Eide, D.J. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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PDBx/mmCIF format | ![]() | 392.6 KB | Display | ![]() |
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PDB format | ![]() | 327.5 KB | Display | ![]() |
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-Validation report
Summary document | ![]() | 347.9 KB | Display | ![]() |
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Full document | ![]() | 500.7 KB | Display | |
Data in XML | ![]() | 30.3 KB | Display | |
Data in CIF | ![]() | 47.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data | |
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Other databases |
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein | Mass: 7419.285 Da / Num. of mol.: 1 / Fragment: two interacting zinc fingers Mutation: three non-canonical cyteines converted to alanines due to oxidative instability Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Description: Zap1 gene derived from pYeF2ZAP1. (Gift from D.J. Eide, University of Wisconsin-Madison). ZZF1-2 portion of gene cloned into pET-21a plasmid (Novagen). Further details can be found in entry citation. Gene: ZAP1 / Plasmid: p21a-zzf1-2 / Species (production host): Escherichia coli / Production host: ![]() ![]() |
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#2: Chemical |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
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NMR experiment |
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NMR details | Text: pulse squences were from the Varian BioPack software package add-on within VNMR two 3D 13C-NOESY-HSQC spectra were recorded in 99% (v/v)D2O with carrier centered on aliphatic (43 ppm) and ...Text: pulse squences were from the Varian BioPack software package add-on within VNMR two 3D 13C-NOESY-HSQC spectra were recorded in 99% (v/v)D2O with carrier centered on aliphatic (43 ppm) and aromatic (125 ppm) regions, respectiviely. |
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Sample preparation
Details | Contents: 0.7 mM protein, 1.5 mM Zn(II), 20 mM MES, 0.2 mM DSS, 1 mM NaN2, 5 mM Beta-mercaptoethanol Solvent system: 90% H2O, 10% D2O or 99% D2O |
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Sample conditions | Ionic strength: no salt / pH: 6.9 / Pressure: 1 atm / Temperature: 293 K |
-NMR measurement
NMR spectrometer | Type: Varian INOVA / Manufacturer: Varian / Model: INOVA / Field strength: 600 MHz |
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Processing
NMR software | Name: CNS / Version: 1.1 Developer: A.T.Brunger, P.D.Adams, G.M.Clore, W.L.Delano, P.Gros, R.W.Grosse-Kunstleve, J.-S.Jiang, J.Kuszewski, M.Nilges, N.S.Pannu, R.J.Read, L.M.Rice, T.Simonson, G.L.Warren Classification: refinement |
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Refinement | Method: torsion angle dynamics, cartesian refinement / Software ordinal: 1 Details: 1443 NOE-derived distance restraints, and 98 dihedral angle restraints. |
NMR representative | Selection criteria: closest to the average |
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 50 / Conformers submitted total number: 20 |