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Yorodumi- PDB-5t1o: Solution-state NMR and SAXS structural ensemble of NPr (1-85) in ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 5t1o | |||||||||
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Title | Solution-state NMR and SAXS structural ensemble of NPr (1-85) in complex with EIN-Ntr (170-424) | |||||||||
Components |
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Keywords | TRANSFERASE / PTSNtr / phosphotransfer / bacterial / complex | |||||||||
Function / homology | Function and homology information transferase activity, transferring phosphorus-containing groups / phosphoenolpyruvate-protein phosphotransferase / phosphoenolpyruvate-protein phosphotransferase activity / phosphoenolpyruvate-dependent sugar phosphotransferase system / : / kinase activity / metal ion binding / cytoplasm Similarity search - Function | |||||||||
Biological species | Escherichia coli O157:H7 (bacteria) Escherichia coli (E. coli) | |||||||||
Method | SOLUTION NMR / SOLUTION SCATTERING / simulated annealing | |||||||||
Authors | Strickland, M. / Stanley, A.M. / Wang, G. / Schwieters, C.D. / Buchanan, S. / Peterkofsky, A. / Tjandra, N. | |||||||||
Funding support | United States, 2items
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Citation | Journal: Structure / Year: 2016 Title: Structure of the NPr:EIN(Ntr) Complex: Mechanism for Specificity in Paralogous Phosphotransferase Systems. Authors: Strickland, M. / Stanley, A.M. / Wang, G. / Botos, I. / Schwieters, C.D. / Buchanan, S.K. / Peterkofsky, A. / Tjandra, N. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5t1o.cif.gz | 2 MB | Display | PDBx/mmCIF format |
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PDB format | pdb5t1o.ent.gz | 1.7 MB | Display | PDB format |
PDBx/mmJSON format | 5t1o.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/t1/5t1o ftp://data.pdbj.org/pub/pdb/validation_reports/t1/5t1o | HTTPS FTP |
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-Related structure data
Related structure data | 5t12C 5t1nC C: citing same article (ref.) |
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Similar structure data | |
Other databases |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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Details | Size exclusion gel filtration was used to determine that this is a 1:1 protein interaction and both proteins are monomers. Small angle X-ray scattering confirmed this and was used as a restraint in the structure calculation |
-Components
#1: Protein | Mass: 9254.570 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli O157:H7 (bacteria) / Gene: ptsO, Z4569, ECs4085 / Plasmid: Plasmid / Details (production host): pETDuet1 / Production host: Escherichia coli (E. coli) / Strain (production host): ER2566 References: UniProt: P0A9N2, UniProt: P0A9N0*PLUS, Transferases; Transferring phosphorus-containing groups; Protein-serine/threonine kinases |
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#2: Protein | Mass: 28380.070 Da / Num. of mol.: 1 / Mutation: H356Q Source method: isolated from a genetically manipulated source Details: This molecule was mutated at position 356 from histidine to glutamine. In E. coli, when the native histidine is present, the sample can be phosphorylated. It was mutated to provide a ...Details: This molecule was mutated at position 356 from histidine to glutamine. In E. coli, when the native histidine is present, the sample can be phosphorylated. It was mutated to provide a homogeneous sample. Additionally, it comprises residues 170-424 of the larger Enzyme I-Ntr molecule. Residue 169 is mutated to glycine due to TEV protease cleavage. Source: (gene. exp.) Escherichia coli (strain K12) (bacteria) Strain: K12 / Gene: ptsP, ygdF, ygdO, b2829, JW2797 / Plasmid: pET28a / Production host: Escherichia coli (E. coli) / Strain (production host): ER2566 References: UniProt: P37177, phosphoenolpyruvate-protein phosphotransferase |
-Experimental details
-Experiment
Experiment |
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NMR experiment |
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-Sample preparation
Details |
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