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- PDB-2y90: Crystal structure of Hfq riboregulator from E. coli (P6 space group) -
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Open data
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Basic information
Entry | Database: PDB / ID: 2y90 | ||||||
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Title | Crystal structure of Hfq riboregulator from E. coli (P6 space group) | ||||||
![]() | PROTEIN HFQ | ||||||
![]() | RNA BINDING PROTEIN / RNA-BINDING PROTEIN / SM-LIKE / RNA CHAPERONE | ||||||
Function / homology | ![]() sRNA-mediated post-transcriptional gene silencing / positive regulation of translation, ncRNA-mediated / RNA folding chaperone / regulation of translation, ncRNA-mediated / bacterial nucleoid / bent DNA binding / regulation of RNA stability / tRNA processing / tRNA binding / regulation of DNA-templated transcription ...sRNA-mediated post-transcriptional gene silencing / positive regulation of translation, ncRNA-mediated / RNA folding chaperone / regulation of translation, ncRNA-mediated / bacterial nucleoid / bent DNA binding / regulation of RNA stability / tRNA processing / tRNA binding / regulation of DNA-templated transcription / DNA binding / RNA binding / ATP binding / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Basquin, J. / Sauter, C. | ||||||
![]() | ![]() Title: Exploiting Protein Engineering and Crystal Polymorphism for Successful X-Ray Structure Determination Authors: Bonnefond, L. / Schellenberger, P. / Basquin, J. / Demangeat, G. / Ritzenthaler, C. / Chenevert, R. / Balg, C. / Frugier, M. / Rudinger-Thirion, J. / Giege, R. / Lorber, L. / Sauter, C. #1: ![]() Title: Sm-Like Proteins in Eubacteria: The Crystal Structure of the Hfq Protein from Escherichia Coli. Authors: Sauter, C. / Basquin, J. / Suck, D. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 26 KB | Display | ![]() |
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PDB format | ![]() | 15.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 2yhtC ![]() 3zxiC ![]() 4v5wC ![]() 1hk9S S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 11307.484 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: Water | ChemComp-HOH / |
Sequence details | TWO AMINO ACIDS ADDED IN N-TERMINUS AND PROBABLE PROTEOLYTIC DEGRADATION AFTER RESIDUE 69. RESIDUES ...TWO AMINO ACIDS ADDED IN N-TERMINUS AND PROBABLE PROTEOLYTI |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 1.7 Å3/Da / Density % sol: 30 % / Description: NONE |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop Details: CRYSTALS WERE OBTAINED BY VAPOR DIFFUSION IN 2UL HANGING DROPS AT 20C. THE RESERVOIR CONTAINED 1.6 M AMMONIUM SULFATE, 0.1 M TRIS-HCL PH 8.0. |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.933 Å / Relative weight: 1 |
Reflection twin | Operator: h,-h-k,-l / Fraction: 0.313 |
Reflection | Resolution: 2.25→54 Å / Num. obs: 2979 / % possible obs: 99 % / Observed criterion σ(I): -3 / Redundancy: 7.6 % / Biso Wilson estimate: 28.6 Å2 / Rmerge(I) obs: 0.06 / Net I/σ(I): 11.7 |
Reflection shell | Resolution: 2.25→2.3 Å / Rmerge(I) obs: 0.17 / Mean I/σ(I) obs: 4.3 / % possible all: 89.3 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1HK9 Resolution: 2.252→53.261 Å / σ(F): 0 / Phase error: 32.43 / Stereochemistry target values: TWIN_LSQ_F Details: THE FULL LENGTH HFQ PROTEIN CRYSTALLIZED AFTER PROTEOLYTIC DEGRADATION AS INDICATED BY THE CRYSTAL SOLVENT SOLVENT CONTENT (SEE REF1). THE RESULTING MONOMER LACKS RESIDUES 70-102. THE LATTER ...Details: THE FULL LENGTH HFQ PROTEIN CRYSTALLIZED AFTER PROTEOLYTIC DEGRADATION AS INDICATED BY THE CRYSTAL SOLVENT SOLVENT CONTENT (SEE REF1). THE RESULTING MONOMER LACKS RESIDUES 70-102. THE LATTER ARE EITHER DISORDERED IN THE CRYSTAL OR ABSENT DUE TO BY PROTEOLYSIS.
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Solvent computation | Shrinkage radii: 0.72 Å / VDW probe radii: 1 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 25.035 Å2 / ksol: 0.333 e/Å3 | ||||||||||||||||||||||||
Displacement parameters | Biso mean: 27.9 Å2
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Refinement step | Cycle: LAST / Resolution: 2.252→53.261 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.2608→24.9582 Å
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