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Yorodumi- PDB-1wbb: Crystal structure of E. coli DNA mismatch repair enzyme MutS, E38... -
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-Basic information
Entry | Database: PDB / ID: 1wbb | ||||||
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Title | Crystal structure of E. coli DNA mismatch repair enzyme MutS, E38A mutant, in complex with a G.T mismatch | ||||||
Components |
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Keywords | DNA-BINDING / ATP-BINDING / DNA BINDING / DNA REPAIR / MISMATCH RECOGNITION | ||||||
Function / homology | Function and homology information adenine/cytosine mispair binding / MutS complex / mismatch repair complex / regulation of DNA recombination / mismatched DNA binding / DNA binding, bending / ATP-dependent DNA damage sensor activity / mismatch repair / ADP binding / damaged DNA binding ...adenine/cytosine mispair binding / MutS complex / mismatch repair complex / regulation of DNA recombination / mismatched DNA binding / DNA binding, bending / ATP-dependent DNA damage sensor activity / mismatch repair / ADP binding / damaged DNA binding / DNA damage response / ATP hydrolysis activity / ATP binding / identical protein binding / cytosol Similarity search - Function | ||||||
Biological species | ESCHERICHIA COLI (E. coli) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.5 Å | ||||||
Authors | Natrajan, G. / Georgijevic, D. / Lebbink, J.H.G. / Winterwerp, H.H.K. / de Wind, N. / Sixma, T.K. | ||||||
Citation | Journal: Embo J. / Year: 2006 Title: Dual Role of Muts Glutamate 38 in DNA Mismatch Discrimination and in the Authorization of Repair. Authors: Lebbink, J.H.G. / Georgijevic, D. / Natrajan, G. / Fish, A. / Winterwerp, H.H.K. / Sixma, T.K. / De Wind, N. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1wbb.cif.gz | 332.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1wbb.ent.gz | 265.3 KB | Display | PDB format |
PDBx/mmJSON format | 1wbb.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1wbb_validation.pdf.gz | 801.3 KB | Display | wwPDB validaton report |
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Full document | 1wbb_full_validation.pdf.gz | 823 KB | Display | |
Data in XML | 1wbb_validation.xml.gz | 55.7 KB | Display | |
Data in CIF | 1wbb_validation.cif.gz | 77.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/wb/1wbb ftp://data.pdbj.org/pub/pdb/validation_reports/wb/1wbb | HTTPS FTP |
-Related structure data
Related structure data | 1wb9C 1wbdC 1e3mS S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
-Protein , 1 types, 2 molecules AB
#1: Protein | Mass: 89546.320 Da / Num. of mol.: 2 / Fragment: RESIDUES 1-800 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ESCHERICHIA COLI (E. coli) / Plasmid: PM800 / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): B834 (BL21) / Variant (production host): PLYSS / References: UniProt: P23909 |
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-DNA chain , 2 types, 2 molecules EF
#2: DNA chain | Mass: 5526.581 Da / Num. of mol.: 1 / Source method: obtained synthetically / Details: G\:T MISMATCH DNA |
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#3: DNA chain | Mass: 5234.382 Da / Num. of mol.: 1 / Source method: obtained synthetically |
-Non-polymers , 3 types, 287 molecules
#4: Chemical | ChemComp-ADP / |
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#5: Chemical | ChemComp-MG / |
#6: Water | ChemComp-HOH / |
-Details
Compound details | ENGINEERED |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.6 Å3/Da / Density % sol: 56.2 % |
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Crystal grow | pH: 7.5 Details: 25 MM HEPES(7.5), 300 MM NACL, 10 MM MGCL2, 14 % PEG 6000., pH 7.50 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID14-1 / Wavelength: 0.93 |
Detector | Type: ADSC CCD / Detector: CCD / Date: Nov 24, 2002 / Details: SAGITAL FOCUSSING GE (220) AND MULTILAYER. |
Radiation | Monochromator: DIAMOND (111), GE (220) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.93 Å / Relative weight: 1 |
Reflection | Resolution: 2.5→20 Å / Num. obs: 75289 / % possible obs: 99.3 % / Redundancy: 3.12 % / Biso Wilson estimate: 53.02 Å2 / Rmerge(I) obs: 0.11 / Net I/σ(I): 9.81 |
Reflection shell | Resolution: 2.5→2.59 Å / Redundancy: 3.06 % / Rmerge(I) obs: 0.72 / Mean I/σ(I) obs: 1.48 / % possible all: 98.3 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1E3M Resolution: 2.5→20 Å / Cor.coef. Fo:Fc: 0.934 / Cor.coef. Fo:Fc free: 0.898 / SU B: 11.618 / SU ML: 0.246 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R: 0.439 / ESU R Free: 0.288 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL PLUS MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 18.08 Å2
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Refinement step | Cycle: LAST / Resolution: 2.5→20 Å
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Refine LS restraints |
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