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- PDB-5jtq: The structure of chaperone SecB in complex with unstructured MBP ... -
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Basic information
Entry | Database: PDB / ID: 5jtq | ||||||
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Title | The structure of chaperone SecB in complex with unstructured MBP binding site d | ||||||
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![]() | CHAPERONE/PROTEIN BINDING / Molecular Chaperone / CHAPERONE-PROTEIN BINDING complex | ||||||
Function / homology | ![]() preprotein binding / maintenance of unfolded protein / protein transport by the Sec complex / carbohydrate transmembrane transporter activity / maltose binding / maltose transport / maltodextrin transmembrane transport / protein targeting / ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing / protein tetramerization ...preprotein binding / maintenance of unfolded protein / protein transport by the Sec complex / carbohydrate transmembrane transporter activity / maltose binding / maltose transport / maltodextrin transmembrane transport / protein targeting / ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing / protein tetramerization / protein localization / unfolded protein binding / protein transport / protein folding / outer membrane-bounded periplasmic space / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR / molecular dynamics | ||||||
![]() | Huang, C. / Saio, T. / Rossi, P. / Kalodimos, C.G. | ||||||
![]() | ![]() Title: Structural basis for the antifolding activity of a molecular chaperone. Authors: Huang, C. / Rossi, P. / Saio, T. / Kalodimos, C.G. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 4.7 MB | Display | ![]() |
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PDB format | ![]() | 4.1 MB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 5jtlC ![]() 5jtmC ![]() 5jtnC ![]() 5jtoC ![]() 5jtpC ![]() 5jtrC C: citing same article ( |
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Similar structure data | |
Other databases |
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein | Mass: 17287.266 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Protein/peptide | Mass: 4879.627 Da / Num. of mol.: 2 / Fragment: residues 108-149 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||
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NMR experiment |
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Sample preparation
Details | Type: solution Contents: 300 uM [U-100% 13C; U-100% 15N] E.coli Chaperone SecB, 300 uM [U-100% 13C; U-100% 15N] E.coli Maltose Binding Protein (MBP) binding site d, 150 mM potassium chloride, 50 mM potassium ...Contents: 300 uM [U-100% 13C; U-100% 15N] E.coli Chaperone SecB, 300 uM [U-100% 13C; U-100% 15N] E.coli Maltose Binding Protein (MBP) binding site d, 150 mM potassium chloride, 50 mM potassium phosphate, 50 mM sodium phosphate, 90% H2O/10% D2O Details: 1H, 13C-ILVMAT-Methyl labelling / Label: Sample_1 / Solvent system: 90% H2O/10% D2O | ||||||||||||||||||||||||
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Sample conditions | Ionic strength: 150 mM / Label: condition_1 / pH: 7 / Pressure: 1 atm / Temperature: 301 K |
-NMR measurement
NMR spectrometer |
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Processing
NMR software |
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Refinement | Method: molecular dynamics / Software ordinal: 1 | |||||||||||||||
NMR representative | Selection criteria: lowest energy | |||||||||||||||
NMR ensemble | Conformer selection criteria: target function / Conformers calculated total number: 100 / Conformers submitted total number: 20 |