5O2K

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

Summary for 5O2K

• Entry DOI: 10.2210/pdb5o2k/pdb
• Descriptor: Probable phosphite transport system-binding protein PtxB (2 entities in total)
• Functional Keywords: phosphite, abc transporters, marine bacteria, pbp, sbp, transport protein
• Biological source: Pseudomonas stutzeri
• Total number of polymer chains: 6
• Total formula weight: 181038.50

Authors

Bisson, C.,Hitchcock, A. (deposition date: 2017-05-21, release date: 2017-12-06, Last modification date: 2024-05-08)

Primary citation

Bisson, C.,Adams, N.B.P.,Stevenson, B.,Brindley, A.A.,Polyviou, D.,Bibby, T.S.,Baker, P.J.,Hunter, C.N.,Hitchcock, A.
The molecular basis of phosphite and hypophosphite recognition by ABC-transporters.
Nat Commun, 8:1746-1746, 2017

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.

PubMed: 29170493
DOI: 10.1038/s41467-017-01226-8

Experimental method

X-RAY DIFFRACTION (2.1 Å)