5T1O

Solution-state NMR and SAXS structural ensemble of NPr (1-85) in complex with EIN-Ntr (170-424)


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 200 
  • Conformers Submitted: 20 
  • Selection Criteria: structures with the lowest energy 

  • Method: SOLUTION SCATTERING

wwPDB Validation   3D Report Full Report


This is version 1.7 of the entry. See complete history


Literature

Structure of the NPr:EIN(Ntr) Complex: Mechanism for Specificity in Paralogous Phosphotransferase Systems.

Strickland, M.Stanley, A.M.Wang, G.Botos, I.Schwieters, C.D.Buchanan, S.K.Peterkofsky, A.Tjandra, N.

(2016) Structure 24: 2127-2137

  • DOI: https://doi.org/10.1016/j.str.2016.10.007
  • Primary Citation of Related Structures:  
    5T12, 5T1N, 5T1O

  • PubMed Abstract: 

    Paralogous enzymes arise from gene duplication events that confer a novel function, although it is unclear how cross-reaction between the original and duplicate protein interaction network is minimized. We investigated HPr:EI sugar and NPr:EI Ntr , the initial complexes of paralogous phosphorylation cascades involved in sugar import and nitrogen regulation in bacteria, respectively. Although the HPr:EI sugar interaction has been well characterized, involving multiple complexes and transient interactions, the exact nature of the NPr:EI Ntr complex was unknown. We set out to identify the key features of the interaction by performing binding assays and elucidating the structure of NPr in complex with the phosphorylation domain of EI Ntr (EIN Ntr ), using a hybrid approach involving X-ray, homology, and sparse nuclear magnetic resonance. We found that the overall fold and active-site structure of the two complexes are conserved in order to maintain productive phosphorylation, however, the interface surface potential differs between the two complexes, which prevents cross-reaction.


  • Organizational Affiliation

    Laboratory of Molecular Biophysics, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Phosphocarrier protein NPr85Escherichia coli O157:H7Mutation(s): 0 
Gene Names: ptsOZ4569ECs4085
EC: 2.7.11
UniProt
Find proteins for P0A9N0 (Escherichia coli (strain K12))
Explore P0A9N0 
Go to UniProtKB:  P0A9N0
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP0A9N0
Sequence Annotations
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  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Phosphoenolpyruvate-protein phosphotransferase PtsP256Escherichia coli K-12Mutation(s): 1 
Gene Names: ptsPygdFygdOb2829JW2797
EC: 2.7.3.9
UniProt
Find proteins for P37177 (Escherichia coli (strain K12))
Explore P37177 
Go to UniProtKB:  P37177
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP37177
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 200 
  • Conformers Submitted: 20 
  • Selection Criteria: structures with the lowest energy 
  • Method: SOLUTION SCATTERING

Structure Validation

View Full Validation Report



Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
National Institutes of Health/National Heart, Lung, and Blood Institute (NIH/NHLBI)United States--
National Institutes of Health/National Institute of Diabetes and Digestive and Kidney Disease (NIH/NIDDK)United States--

Revision History  (Full details and data files)

  • Version 1.0: 2016-11-16
    Type: Initial release
  • Version 1.1: 2016-12-07
    Changes: Database references
  • Version 1.2: 2016-12-21
    Changes: Database references
  • Version 1.3: 2017-09-20
    Changes: Author supporting evidence, Data collection, Structure summary
  • Version 1.4: 2017-11-01
    Changes: Author supporting evidence, Structure summary
  • Version 1.5: 2019-05-08
    Changes: Data collection, Database references, Experimental preparation
  • Version 1.6: 2019-12-04
    Changes: Author supporting evidence, Data collection
  • Version 1.7: 2023-06-14
    Changes: Database references, Other