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- PDB-4g0x: Crystal Structure of Arabidopsis thaliana AGO1 MID domain -

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Basic information

Entry
Database: PDB / ID: 4g0x
TitleCrystal Structure of Arabidopsis thaliana AGO1 MID domain
ComponentsProtein argonaute 1
KeywordsGENE REGULATION / MID domain / small RNA 5' nucleotide recognition
Function / homology
Function and homology information


adaxial/abaxial pattern specification / adventitious root development / auxin metabolic process / leaf morphogenesis / leaf proximal/distal pattern formation / RNAi-mediated antiviral immune response / leaf vascular tissue pattern formation / response to far red light / post-transcriptional gene silencing / response to auxin ...adaxial/abaxial pattern specification / adventitious root development / auxin metabolic process / leaf morphogenesis / leaf proximal/distal pattern formation / RNAi-mediated antiviral immune response / leaf vascular tissue pattern formation / response to far red light / post-transcriptional gene silencing / response to auxin / miRNA-mediated post-transcriptional gene silencing / siRNA binding / miRNA binding / RNA endonuclease activity / regulation of translation / defense response to virus / cell differentiation / ribonucleoprotein complex / mRNA binding / innate immune response / metal ion binding / nucleus / cytoplasm
Similarity search - Function
Argonaut, glycine-rich domain / Glycine-rich region of argonaut / Protein argonaute, Mid domain / Argonaute-like, PIWI domain / Mid domain of argonaute / Argonaute linker 2 domain / Protein argonaute, N-terminal / N-terminal domain of argonaute / Argonaute linker 2 domain / DUF1785 ...Argonaut, glycine-rich domain / Glycine-rich region of argonaut / Protein argonaute, Mid domain / Argonaute-like, PIWI domain / Mid domain of argonaute / Argonaute linker 2 domain / Protein argonaute, N-terminal / N-terminal domain of argonaute / Argonaute linker 2 domain / DUF1785 / Argonaute, linker 1 domain / Argonaute linker 1 domain / Piwi domain / Piwi domain profile. / Piwi domain / Piwi / PAZ domain superfamily / PAZ / PAZ domain / PAZ domain / PAZ domain profile. / Response regulator / Ribonuclease H superfamily / Ribonuclease H-like superfamily / Rossmann fold / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
Biological speciesArabidopsis thaliana (thale cress)
MethodX-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 1.35 Å
AuthorsFrank, F. / Hauver, J. / Sonenberg, N. / Nagar, B.
CitationJournal: Embo J. / Year: 2012
Title: Arabidopsis Argonaute MID domains use their nucleotide specificity loop to sort small RNAs.
Authors: Frank, F. / Hauver, J. / Sonenberg, N. / Nagar, B.
History
DepositionJul 10, 2012Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jul 25, 2012Provider: repository / Type: Initial release
Revision 1.1Aug 29, 2012Group: Database references
Revision 1.2Sep 12, 2012Group: Database references

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Protein argonaute 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)17,1546
Polymers16,6741
Non-polymers4805
Water3,117173
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)37.250, 60.973, 67.809
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

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Components

#1: Protein Protein argonaute 1


Mass: 16673.633 Da / Num. of mol.: 1 / Fragment: MID domain, UNP residues 593-738
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Arabidopsis thaliana (thale cress) / Gene: AGO1, At1g48410, F11A17.3, T1N15.2 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 DE3 / References: UniProt: O04379
#2: Chemical
ChemComp-SO4 / SULFATE ION / Sulfate


Mass: 96.063 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: SO4
#3: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 173 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 2.31 Å3/Da / Density % sol: 46.73 %
Crystal growTemperature: 277 K / Method: vapor diffusion, hanging drop / pH: 4.5
Details: 0.1 M citric acid, 2 M ammonium sulfate, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K

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Data collection

DiffractionMean temperature: 200 K
Diffraction sourceSource: SYNCHROTRON / Site: CLSI / Beamline: 08B1-1 / Wavelength: 0.9792 Å
DetectorType: RAYONIX MX300HE / Detector: CCD / Date: Feb 27, 2010
RadiationMonochromator: KOHZU double crystal monochromator / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9792 Å / Relative weight: 1
ReflectionResolution: 1.35→30 Å / Num. all: 36996 / Num. obs: 35331 / % possible obs: 95.5 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3
Reflection shellResolution: 1.35→1.4 Å / % possible all: 71.9

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Processing

Software
NameVersionClassification
HKL-2000data collection
PHENIX(phenix.refine: 1.5_2)model building
PHENIX(phenix.refine: 1.5_2)refinement
HKL-2000data reduction
HKL-2000data scaling
PHENIX1.5_2phasing
RefinementMethod to determine structure: SAD / Resolution: 1.35→22.67 Å / SU ML: 0.25 / σ(F): 1.34 / Phase error: 16.38 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.1788 3527 5.63 %
Rwork0.1623 --
obs0.1632 62602 95.5 %
all-38732 -
Solvent computationShrinkage radii: 0.86 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 40 Å2 / ksol: 0.4 e/Å3
Displacement parameters
Baniso -1Baniso -2Baniso -3
1--2.2111 Å2-0 Å20 Å2
2---4.9042 Å2-0 Å2
3---6.4266 Å2
Refinement stepCycle: LAST / Resolution: 1.35→22.67 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1146 0 25 173 1344
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0111241
X-RAY DIFFRACTIONf_angle_d1.3521695
X-RAY DIFFRACTIONf_dihedral_angle_d15.489485
X-RAY DIFFRACTIONf_chiral_restr0.074196
X-RAY DIFFRACTIONf_plane_restr0.006215
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.35-1.36850.19721030.19131656X-RAY DIFFRACTION67
1.3685-1.3880.20691100.18521857X-RAY DIFFRACTION73
1.388-1.40880.20651170.18591938X-RAY DIFFRACTION80
1.4088-1.43080.19051290.17382180X-RAY DIFFRACTION87
1.4308-1.45420.21461350.16472256X-RAY DIFFRACTION91
1.4542-1.47930.19841390.15812311X-RAY DIFFRACTION94
1.4793-1.50620.16681420.15842377X-RAY DIFFRACTION96
1.5062-1.53520.16141530.15442449X-RAY DIFFRACTION99
1.5352-1.56650.17851470.15382461X-RAY DIFFRACTION100
1.5665-1.60050.16241470.1552459X-RAY DIFFRACTION100
1.6005-1.63780.17861470.14672485X-RAY DIFFRACTION100
1.6378-1.67870.17181430.1532498X-RAY DIFFRACTION100
1.6787-1.72410.18861470.15142464X-RAY DIFFRACTION100
1.7241-1.77480.16541440.15072469X-RAY DIFFRACTION100
1.7748-1.83210.17081500.14862478X-RAY DIFFRACTION100
1.8321-1.89750.19981510.14782473X-RAY DIFFRACTION100
1.8975-1.97340.17881490.15322477X-RAY DIFFRACTION100
1.9734-2.06320.17071480.14692468X-RAY DIFFRACTION100
2.0632-2.17190.16921490.14742458X-RAY DIFFRACTION100
2.1719-2.30780.19571470.14972477X-RAY DIFFRACTION100
2.3078-2.48580.15731460.15862489X-RAY DIFFRACTION100
2.4858-2.73560.1951460.16652476X-RAY DIFFRACTION100
2.7356-3.13060.15511450.17262471X-RAY DIFFRACTION100
3.1306-3.94080.19611480.16132473X-RAY DIFFRACTION100
3.9408-22.67280.17261450.192475X-RAY DIFFRACTION100

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