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Yorodumi- PDB-1mdp: REFINED STRUCTURES OF TWO INSERTION(SLASH)DELETION MUTANTS PROBE ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1mdp | |||||||||
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Title | REFINED STRUCTURES OF TWO INSERTION(SLASH)DELETION MUTANTS PROBE FUNCTION OF THE MALTODEXTRIN BINDING PROTEIN | |||||||||
Components | MALTODEXTRIN BINDING PROTEIN | |||||||||
Keywords | 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 / Resolution: 2.3 Å | |||||||||
Authors | Sharff, A.J. / Quiocho, F.A. | |||||||||
Citation | Journal: J.Mol.Biol. / Year: 1995 Title: Refined structures of two insertion/deletion mutants probe function of the maltodextrin binding protein. Authors: Sharff, A.J. / Rodseth, L.E. / Szmelcman, S. / Hofnung, M. / Quiocho, F.A. #1: Journal: Biochemistry / Year: 1992 Title: Crystallographic Evidence of a Large Ligand-Induced Hinge-Twist Motion between the Two Domains of the Maltodextrin Binding Protein Involved in Transport and Chemotaxis Authors: Sharff, A.J. / Rodseth, L.E. / Spurlino, J.C. / Quiocho, F.A. #2: Journal: J.Biol.Chem. / Year: 1991 Title: The 2.3 Angstroms Resolution Structure of the Maltose-or Maltodextrin-Binding Protein, a Primary Receptor of Bacterial Active Transport and Chemotaxis Authors: Spurlino, J.C. / Lu, G.-Y. / Quiocho, F.A. #3: Journal: J.Mol.Biol. / Year: 1987 Title: Silent and Functional Changes in the Periplasmic Maltose-Binding Protein of Escherichia Coli K12 II. Chemotaxis Towards Maltose Authors: Duplay, P. / Szmelcman, S. #4: Journal: J.Mol.Biol. / Year: 1987 Title: Silent and Functional Changes in the Periplasmic Maltose-Binding Protein of Escherichia Coli K12 I. Transport of Maltose Authors: Duplay, P. / Szmelcman, S. / Bedouelle, H. / Hofnung, M. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1mdp.cif.gz | 152.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1mdp.ent.gz | 119.8 KB | Display | PDB format |
PDBx/mmJSON format | 1mdp.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1mdp_validation.pdf.gz | 503 KB | Display | wwPDB validaton report |
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Full document | 1mdp_full_validation.pdf.gz | 514 KB | Display | |
Data in XML | 1mdp_validation.xml.gz | 16.3 KB | Display | |
Data in CIF | 1mdp_validation.cif.gz | 25.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/md/1mdp ftp://data.pdbj.org/pub/pdb/validation_reports/md/1mdp | HTTPS FTP |
-Related 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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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (0.1615, -0.652099, -0.740699), Vector: |
-Components
#1: Protein | Mass: 39965.148 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / References: UniProt: P02928, UniProt: P0AEX9*PLUS #2: Polysaccharide | #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.31 Å3/Da / Density % sol: 46.86 % | |||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 4.5 / Method: vapor diffusion, hanging dropDetails: microseeding into drops of 18-20 % PEG over 18-25 % PEG | |||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | Num. obs: 39720 / % possible obs: 74 % / Observed criterion σ(I): 2 |
Reflection | *PLUS Highest resolution: 2.25 Å / Num. measured all: 62502 / Rmerge(I) obs: 0.0421 |
-Processing
Software |
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Refinement | Resolution: 2.3→10 Å / σ(F): 2 /
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Refinement step | Cycle: LAST / Resolution: 2.3→10 Å
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Refine LS restraints |
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Software | *PLUS Name: X-PLOR/PROLSQ / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.187 / Rfactor Rwork: 0.187 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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