5O2K

Native apo-structure of Pseudomonas stutzeri PtxB to 2.1 A resolution


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.10 Å
  • R-Value Free: 0.282 
  • R-Value Work: 0.236 
  • R-Value Observed: 0.239 

wwPDB Validation   3D Report Full Report


This is version 1.1 of the entry. See complete history


Literature

The molecular basis of phosphite and hypophosphite recognition by ABC-transporters.

Bisson, C.Adams, N.B.P.Stevenson, B.Brindley, A.A.Polyviou, D.Bibby, T.S.Baker, P.J.Hunter, C.N.Hitchcock, A.

(2017) Nat Commun 8: 1746-1746

  • DOI: https://doi.org/10.1038/s41467-017-01226-8
  • Primary Citation of Related Structures:  
    5JVB, 5LQ1, 5LQ5, 5LQ8, 5LV1, 5ME4, 5O2J, 5O2K, 5O37

  • PubMed Abstract: 

    Inorganic phosphate is the major bioavailable form of the essential nutrient phosphorus. However, the concentration of phosphate in most natural habitats is low enough to limit microbial growth. Under phosphate-depleted conditions some bacteria utilise phosphite and hypophosphite as alternative sources of phosphorus, but the molecular basis of reduced phosphorus acquisition from the environment is not fully understood. Here, we present crystal structures and ligand binding affinities of periplasmic binding proteins from bacterial phosphite and hypophosphite ATP-binding cassette transporters. We reveal that phosphite and hypophosphite specificity results from a combination of steric selection and the presence of a P-H…π interaction between the ligand and a conserved aromatic residue in the ligand-binding pocket. The characterisation of high affinity and specific transporters has implications for the marine phosphorus redox cycle, and might aid the use of phosphite as an alternative phosphorus source in biotechnological, industrial and agricultural applications.


  • Organizational Affiliation

    Department of Molecular Biology and Biotechnology, University of Sheffield, Firth Court, Western Bank, Sheffield, S10 2TN, UK.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Probable phosphite transport system-binding protein PtxB273Stutzerimonas stutzeriMutation(s): 0 
Gene Names: ptxB
UniProt
Find proteins for O69052 (Stutzerimonas stutzeri)
Explore O69052 
Go to UniProtKB:  O69052
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupO69052
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.10 Å
  • R-Value Free: 0.282 
  • R-Value Work: 0.236 
  • R-Value Observed: 0.239 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 87.947α = 90
b = 136.64β = 115.02
c = 90.843γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
xia2data reduction
xia2data scaling
PHASERphasing

Structure Validation

View Full Validation Report



Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
Biotechnology and Biological Sciences Research CouncilUnited KingdomBB/M000265/1
Biotechnology and Biological Sciences Research CouncilUnited KingdomBB/M011305/1
European Research Council338895
European Union283570
Diamond Light SourceBAG applications MX-8987 and MX-12788

Revision History  (Full details and data files)

  • Version 1.0: 2017-12-06
    Type: Initial release
  • Version 1.1: 2024-05-08
    Changes: Data collection, Database references