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Yorodumi- PDB-1lax: CRYSTAL STRUCTURE OF MALE31, A DEFECTIVE FOLDING MUTANT OF MALTOS... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1lax | |||||||||
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Title | CRYSTAL STRUCTURE OF MALE31, A DEFECTIVE FOLDING MUTANT OF MALTOSE-BINDING PROTEIN | |||||||||
Components | MALTOSE-BINDING PROTEIN MUTANT MALE31 | |||||||||
Keywords | SUGAR BINDING PROTEIN / misfolding mutant / sugar transport | |||||||||
Function / homology | Function and homology information detection of maltose stimulus / maltose transport complex / carbohydrate transport / carbohydrate transmembrane transporter activity / maltose binding / maltose transport / maltodextrin transmembrane transport / ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing / ATP-binding cassette (ABC) transporter complex / cell chemotaxis ...detection of maltose stimulus / maltose transport complex / carbohydrate transport / carbohydrate transmembrane transporter activity / maltose binding / maltose transport / maltodextrin transmembrane transport / ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing / ATP-binding cassette (ABC) transporter complex / cell chemotaxis / outer membrane-bounded periplasmic space / periplasmic space / DNA damage response / membrane Similarity search - Function | |||||||||
Biological species | Escherichia coli (E. coli) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.85 Å | |||||||||
Authors | Saul, F.A. / Mourez, M. / Vulliez-le Normand, B. / Sassoon, N. / Bentley, G.A. / Betton, J.M. | |||||||||
Citation | Journal: PROTEIN SCI. / Year: 2003 Title: Crystal structure of a defective folding protein Authors: Saul, F.A. / Mourez, M. / Vulliez-le Normand, B. / Sassoon, N. / Bentley, G.A. / Betton, J.M. #1: Journal: J.Biol.Chem. / Year: 1998 Title: Degradation versus aggregation of misfolded maltose-binding protein in the periplasm of Escherichia coli Authors: Betton, J.M. / Sassoon, N. / Hofnung, M. / Laurent, M. #2: Journal: J.Biol.Chem. / Year: 1996 Title: Folding of a mutant maltose-binding protein of Escherichia coli which forms inclusion bodies Authors: Betton, J.M. / Hofnung, M. | |||||||||
History |
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Remark 600 | Heterogen Atoms O1 of GLC B 401 and GLC D 401 are missing |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1lax.cif.gz | 171.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1lax.ent.gz | 134.3 KB | Display | PDB format |
PDBx/mmJSON format | 1lax.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1lax_validation.pdf.gz | 1.2 MB | Display | wwPDB validaton report |
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Full document | 1lax_full_validation.pdf.gz | 1.2 MB | Display | |
Data in XML | 1lax_validation.xml.gz | 35.4 KB | Display | |
Data in CIF | 1lax_validation.cif.gz | 54.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/la/1lax ftp://data.pdbj.org/pub/pdb/validation_reports/la/1lax | HTTPS FTP |
-Related structure data
Related structure data | 1anfS S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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-Components
#1: Protein | Mass: 40795.145 Da / Num. of mol.: 2 / Fragment: MALE31 / Mutation: G32D I33P Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Gene: MALE / Production host: Escherichia coli (E. coli) / Strain (production host): MC4100 Derivative / References: UniProt: P02928, UniProt: P0AEX9*PLUS #2: Polysaccharide | #3: Water | ChemComp-HOH / | |
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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: 2.2 Å3/Da / Density % sol: 44.15 % | ||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 290 K / Method: vapor diffusion, hanging drop / pH: 8.5 Details: PEG 4000, TRIS/HCl, ISOPROPANOL, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 290K | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 17 ℃ | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 110 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID14-3 / Wavelength: 0.931 Å |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Jun 19, 2000 |
Radiation | Monochromator: Diamond(111), Ge(220) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.931 Å / Relative weight: 1 |
Reflection | Resolution: 1.85→26 Å / Num. all: 60245 / Num. obs: 60245 / % possible obs: 99.8 % / Redundancy: 7.5 % / Rmerge(I) obs: 0.058 / Net I/σ(I): 9.2 |
Reflection shell | Resolution: 1.85→1.95 Å / Redundancy: 6.9 % / Rmerge(I) obs: 0.201 / Mean I/σ(I) obs: 3.4 / Num. unique all: 8705 / % possible all: 99.2 |
Reflection | *PLUS Lowest resolution: 26 Å |
Reflection shell | *PLUS % possible obs: 99.2 % / Num. unique obs: 8670 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1ANF Resolution: 1.85→26 Å / SU B: 3.703 / SU ML: 0.116 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.137 / ESU R Free: 0.129 / Stereochemistry target values: maximum likelihood
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Displacement parameters | Biso mean: 13.71 Å2
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Refinement step | Cycle: LAST / Resolution: 1.85→26 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.85→1.873 Å / Total num. of bins used: 40
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Refinement | *PLUS % reflection Rfree: 5 % / Rfactor Rfree: 0.202 / Rfactor Rwork: 0.157 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |