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Yorodumi- PDB-2lbs: Solution structure of double-stranded RNA binding domain of S. ce... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2lbs | ||||||
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Title | Solution structure of double-stranded RNA binding domain of S. cerevisiae RNase III (Rnt1p) in complex with AAGU tetraloop hairpin | ||||||
Components |
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Keywords | HYDROLASE/RNA / dsRBD / AAGU tetraloop / HYDROLASE-RNA complex | ||||||
Function / homology | Function and homology information box C/D sno(s)RNA processing / box H/ACA sno(s)RNA processing / regulation of fungal-type cell wall organization / termination of RNA polymerase II transcription, exosome-dependent / U1 snRNA 3'-end processing / U5 snRNA 3'-end processing / U4 snRNA 3'-end processing / ribonuclease III / ribonuclease III activity / termination of RNA polymerase II transcription ...box C/D sno(s)RNA processing / box H/ACA sno(s)RNA processing / regulation of fungal-type cell wall organization / termination of RNA polymerase II transcription, exosome-dependent / U1 snRNA 3'-end processing / U5 snRNA 3'-end processing / U4 snRNA 3'-end processing / ribonuclease III / ribonuclease III activity / termination of RNA polymerase II transcription / rRNA transcription / rRNA processing / double-stranded RNA binding / chromatin organization / nucleolus / nucleoplasm / nucleus Similarity search - Function | ||||||
Biological species | Saccharomyces cerevisiae (brewer's yeast) | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Model details | lowest energy, model 1 | ||||||
Authors | Wang, Z. / Hartman, E. / Roy, K. / Chanfreau, G. / Feigon, J. | ||||||
Citation | Journal: Structure / Year: 2011 Title: Structure of a Yeast RNase III dsRBD Complex with a Noncanonical RNA Substrate Provides New Insights into Binding Specificity of dsRBDs. Authors: Wang, Z. / Hartman, E. / Roy, K. / Chanfreau, G. / Feigon, J. #1: Journal: Proc.Natl.Acad.Sci.USA / Year: 2004 Title: Structural basis for recognition of the AGNN tetraloop RNA fold by the double-stranded RNA-binding domain of Rnt1p RNase III Authors: Wu, H. / Henras, A. / Chanfreau, G. / Feigon, J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2lbs.cif.gz | 759.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2lbs.ent.gz | 657.4 KB | Display | PDB format |
PDBx/mmJSON format | 2lbs.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/lb/2lbs ftp://data.pdbj.org/pub/pdb/validation_reports/lb/2lbs | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: RNA chain | Mass: 10282.124 Da / Num. of mol.: 1 / Source method: obtained synthetically |
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#2: Protein | Mass: 9822.364 Da / Num. of mol.: 1 / Fragment: DRBM domain residues 366-453 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast) Gene: RNT1, YM9408.01C, YM9959.21, YMR239C / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 / References: UniProt: Q02555, ribonuclease III |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details |
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Sample |
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Sample conditions | Ionic strength: 0.15 / pH: 6.5 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: torsion angle dynamics / Software ordinal: 1 | ||||||||||||||||||||||||||||||||||||||||||||
NMR constraints | NOE constraints total: 3600 / NOE intraresidue total count: 1085 / NOE long range total count: 467 / NOE medium range total count: 415 / NOE sequential total count: 823 | ||||||||||||||||||||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 16 |