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- PDB-3gs3: Structure of the N-terminal HEAT Domain of Symplekin from D. mela... -

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Basic information

Entry
Database: PDB / ID: 3gs3
TitleStructure of the N-terminal HEAT Domain of Symplekin from D. melanogaster
ComponentsSymplekin
KeywordsTranscription / Protein Binding / helix-turn-helix HEAT repeat extended loop
Function / homology
Function and homology information


Processing of Intronless Pre-mRNAs / histone locus body / mRNA 3'-end processing / Processing of Capped Intron-Containing Pre-mRNA / tricellular tight junction / RNA Polymerase II Transcription Termination / Transport of Mature mRNA Derived from an Intronless Transcript / mRNA 3'-end processing by stem-loop binding and cleavage / co-transcriptional mRNA 3'-end processing, cleavage and polyadenylation pathway / mRNA cleavage and polyadenylation specificity factor complex ...Processing of Intronless Pre-mRNAs / histone locus body / mRNA 3'-end processing / Processing of Capped Intron-Containing Pre-mRNA / tricellular tight junction / RNA Polymerase II Transcription Termination / Transport of Mature mRNA Derived from an Intronless Transcript / mRNA 3'-end processing by stem-loop binding and cleavage / co-transcriptional mRNA 3'-end processing, cleavage and polyadenylation pathway / mRNA cleavage and polyadenylation specificity factor complex / RNA binding / nucleus
Similarity search - Function
Symplekin/Pta1 / Symplekin C-terminal / Symplekin/Pta1, N-terminal / Symplekin/PTA1 N-terminal / Symplekin tight junction protein C terminal / Leucine-rich Repeat Variant / Leucine-rich Repeat Variant / Armadillo-like helical / Alpha Horseshoe / Armadillo-type fold / Mainly Alpha
Similarity search - Domain/homology
Biological speciesDrosophila melanogaster (fruit fly)
MethodX-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 2.4 Å
AuthorsKennedy, S.A. / Redinbo, M.R.
CitationJournal: J.Mol.Biol. / Year: 2009
Title: Crystal structure of the HEAT domain from the Pre-mRNA processing factor Symplekin.
Authors: Kennedy, S.A. / Frazier, M.L. / Steiniger, M. / Mast, A.M. / Marzluff, W.F. / Redinbo, M.R.
History
DepositionMar 26, 2009Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jul 14, 2009Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Feb 21, 2024Group: Data collection / Database references / Category: chem_comp_atom / chem_comp_bond / database_2
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Symplekin


Theoretical massNumber of molelcules
Total (without water)28,3151
Polymers28,3151
Non-polymers00
Water2,468137
1
A: Symplekin

A: Symplekin


Theoretical massNumber of molelcules
Total (without water)56,6292
Polymers56,6292
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation7_645y+1,x-1,-z1
Buried area1260 Å2
ΔGint-17 kcal/mol
Surface area23700 Å2
MethodPISA
Unit cell
Length a, b, c (Å)68.336, 68.336, 139.340
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number92
Space group name H-MP41212

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Components

#1: Protein Symplekin / LD45768p


Mass: 28314.590 Da / Num. of mol.: 1 / Fragment: residues 19-270
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Drosophila melanogaster (fruit fly) / Gene: CG2097, Dmel_CG2097 / Plasmid: pMCGS9 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 DE3 GOLD / References: UniProt: Q8MSU4
#2: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 137 / 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: 2

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Sample preparation

CrystalDensity Matthews: 2.87 Å3/Da / Density % sol: 57.18 %
Crystal growTemperature: 295 K / Method: vapor diffusion, hanging drop / pH: 8
Details: 27% PEG 3350 0.425 M sodium citrate 10 mM HEPES 1 mM DTT 0.01% sodium azide , pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K

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Data collection

Diffraction
IDMean temperature (K)Crystal-ID
11001
21
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 22-BM / Wavelength: 0.97190, 0.97958
DetectorType: MAR CCD 165 mm / Detector: CCD / Date: Jun 18, 2007
Radiation
IDProtocolMonochromatic (M) / Laue (L)Scattering typeWavelength-ID
1SINGLE WAVELENGTHMx-ray1
2SINGLE WAVELENGTHMx-ray1
Radiation wavelength
IDWavelength (Å)Relative weight
10.97191
20.979581
ReflectionResolution: 2.4→50 Å / Num. all: 13568 / Num. obs: 12295 / % possible obs: 90.6 % / Observed criterion σ(F): 1 / Observed criterion σ(I): 2 / Redundancy: 6.4 % / Net I/σ(I): 24.7
Reflection shellResolution: 2.4→2.49 Å / Redundancy: 2.8 % / Mean I/σ(I) obs: 1.9 / % possible all: 79.6

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Processing

Software
NameVersionClassification
HKL-2000data collection
SOLVEphasing
CNS1.1refinement
HKL-2000data reduction
HKL-2000data scaling
RefinementMethod to determine structure: SAD / Resolution: 2.4→50 Å / σ(F): 0 / Stereochemistry target values: Engh & Huber
RfactorNum. reflection% reflectionSelection details
Rfree0.2653 876 -Random
Rwork0.2068 ---
all0.2068 13568 --
obs0.2068 12295 90.6 %-
Refinement stepCycle: LAST / Resolution: 2.4→50 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1922 0 0 137 2059

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