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- PDB-2p4v: Crystal structure of the transcript cleavage factor, GreB at 2.6A... -

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Basic information

Entry
Database: PDB / ID: 2p4v
TitleCrystal structure of the transcript cleavage factor, GreB at 2.6A resolution
ComponentsTranscription elongation factor greB
KeywordsTRANSCRIPTION / transcript cleavage / Gre-factors / RNA polymerase
Function / homology
Function and homology information


DNA-templated transcription elongation / transcription elongation factor activity / RNA polymerase binding / regulation of DNA-templated transcription elongation / DNA-templated transcription initiation / DNA binding
Similarity search - Function
Transcription elongation factor GreB / Transcription elongation factor GreA/GreB / Prokaryotic transcription elongation factors signature 1. / Transcription elongation factor, GreA/GreB, N-terminal domain / Transcription elongation factor, GreA/GreB, C-terminal domain / Transcription elongation factor, GreA/GreB, conserved site / Transcription elongation factor, GreA/GreB, N-terminal / Transcription elongation factor, GreA/GreB, N-terminal domain superfamily / Transcription elongation factor, N-terminal / Prokaryotic transcription elongation factors signature 2. ...Transcription elongation factor GreB / Transcription elongation factor GreA/GreB / Prokaryotic transcription elongation factors signature 1. / Transcription elongation factor, GreA/GreB, N-terminal domain / Transcription elongation factor, GreA/GreB, C-terminal domain / Transcription elongation factor, GreA/GreB, conserved site / Transcription elongation factor, GreA/GreB, N-terminal / Transcription elongation factor, GreA/GreB, N-terminal domain superfamily / Transcription elongation factor, N-terminal / Prokaryotic transcription elongation factors signature 2. / Transcription elongation factor, GreA/GreB, C-terminal / Transcription elongation factor GreA/GreB family / Transcription elongation factor, GreA/GreB, C-term / Transcription elongation factor GreA/GreB, C-terminal domain superfamily / Chitinase A; domain 3 / Helix Hairpins / Roll / Orthogonal Bundle / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
Transcription elongation factor GreB / Transcription elongation factor GreB
Similarity search - Component
Biological speciesEscherichia coli (E. coli)
MethodX-RAY DIFFRACTION / SYNCHROTRON / Single Wavelength / Resolution: 2.6 Å
AuthorsVassylyeva, M.N. / Svetlov, V. / Dearborn, A.D. / Klyuyev, S. / Artsimovitch, I. / Vassylyev, D.G.
CitationJournal: Embo Rep. / Year: 2007
Title: The carboxy-terminal coiled-coil of the RNA polymerase beta'-subunit is the main binding site for Gre factors.
Authors: Vassylyeva, M.N. / Svetlov, V. / Dearborn, A.D. / Klyuyev, S. / Artsimovitch, I. / Vassylyev, D.G.
History
DepositionMar 13, 2007Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jan 22, 2008Provider: 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

Downloads & links

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Assembly

Deposited unit
A: Transcription elongation factor greB
B: Transcription elongation factor greB
C: Transcription elongation factor greB
D: Transcription elongation factor greB
E: Transcription elongation factor greB
F: Transcription elongation factor greB


Theoretical massNumber of molelcules
Total (without water)111,4396
Polymers111,4396
Non-polymers00
Water5,999333
1
A: Transcription elongation factor greB


Theoretical massNumber of molelcules
Total (without water)18,5731
Polymers18,5731
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: Transcription elongation factor greB


Theoretical massNumber of molelcules
Total (without water)18,5731
Polymers18,5731
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
C: Transcription elongation factor greB


Theoretical massNumber of molelcules
Total (without water)18,5731
Polymers18,5731
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
4
D: Transcription elongation factor greB


Theoretical massNumber of molelcules
Total (without water)18,5731
Polymers18,5731
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
5
E: Transcription elongation factor greB


Theoretical massNumber of molelcules
Total (without water)18,5731
Polymers18,5731
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
6
F: Transcription elongation factor greB


Theoretical massNumber of molelcules
Total (without water)18,5731
Polymers18,5731
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)148.320, 148.320, 116.770
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number78
Space group name H-MP43
DetailsThe monomer is a bilogical assembly of the protein

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Components

#1: Protein
Transcription elongation factor greB / Transcript cleavage factor greB


Mass: 18573.109 Da / Num. of mol.: 6
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli) / Strain: DH5alpha / Gene: greB / Plasmid: bpIA577 / Species (production host): Escherichia coli / Production host: Escherichia coli BL21 (bacteria) / Strain (production host): BL21 / References: UniProt: P64273, UniProt: P30128*PLUS
#2: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 333 / 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

Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 6.5
Details: 3.75% PEG 8000, 25 mM ammonium sulfate, 12 mM sodium cacodylate, 8mM TRIS HCl, 800 mM NaCl, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: Photon Factory / Beamline: AR-NW12A / Wavelength: 0.9794 Å
DetectorType: ADSC QUANTUM 210 / Detector: CCD / Date: Oct 14, 2004
RadiationMonochromator: Graphite / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9794 Å / Relative weight: 1
ReflectionResolution: 2.6→30 Å / Num. all: 74091 / Num. obs: 74091 / % possible obs: 95.3 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 6.4 % / Biso Wilson estimate: 42 Å2 / Rmerge(I) obs: 0.057 / Rsym value: 0.057 / Net I/σ(I): 32.6
Reflection shellResolution: 2.6→2.69 Å / Redundancy: 3 % / Rmerge(I) obs: 0.498 / Mean I/σ(I) obs: 2.8 / Num. unique all: 5540 / Rsym value: 0.498 / % possible all: 73

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Processing

Software
NameVersionClassification
ADSCQuantumdata collection
MLPHAREphasing
CNS1refinement
HKL-2000data reduction
HKL-2000data scaling
RefinementMethod to determine structure: Single Wavelength / Resolution: 2.6→10 Å / Isotropic thermal model: isotropic / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
Details: THE PERFECT MEROHEDRAL TWINNING WAS DETECTED IN THE CRYSTALS WITH THE TWINNING OPERATOR {H,-K,-L}. THE REFINEMENT STATISTICS PRESENTED FOR THIS ENTRY CORRESPONDS TO THE REFINEMENT CARRIED ...Details: THE PERFECT MEROHEDRAL TWINNING WAS DETECTED IN THE CRYSTALS WITH THE TWINNING OPERATOR {H,-K,-L}. THE REFINEMENT STATISTICS PRESENTED FOR THIS ENTRY CORRESPONDS TO THE REFINEMENT CARRIED OUT USING THE TWINNING OPTION OF THE CNS PROGRAM. FOR THE DEPOSITION THE DIFFRACTION DATA WERE DETWINNED USING THE CNS PROGRAM. THEREFORE, SOME REFLECTIONS WERE LOST DUE TO THE DETWINNING PROCEDURE AND ARE MISSING IN THE DEPOSITED SF FILE, WHEREAS THE REFINEMENT STATISTICS CALCULATED BASED ON THE DETWINNED ATA MIGHT BE SLIGHTLY DIFFERENT FROM THOSE OBTAINED DURING THE "TWINNED" REFINEMENT INCLUDED IN THIS ENTRY.
RfactorNum. reflectionSelection details
Rfree0.257 4318 random
Rwork0.226 --
all0.23 72792 -
obs0.23 72792 -
Displacement parametersBiso mean: 42.5 Å2
Refinement stepCycle: LAST / Resolution: 2.6→10 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms7752 0 0 333 8085
Refine LS restraints
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONc_bond_d0.015
X-RAY DIFFRACTIONc_angle_deg1.79
X-RAY DIFFRACTIONc_improper_angle_d0.83
LS refinement shellResolution: 2.6→2.69 Å
RfactorNum. reflection% reflection
Rfree0.28 320 -
Rwork0.271 --
obs-5540 73 %

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