5JVB

1.95A resolution structure of PtxB from Trichodesmium erythraeum IMS101 in complex with phosphite

Summary for 5JVB

• Entry DOI: 10.2210/pdb5jvb/pdb
• Descriptor: Phosphonate ABC transporter, periplasmic phosphonate-binding protein, PHOSPHONATE (3 entities in total)
• Functional Keywords: periplasmic binding protein (pbp), phosphite transpoter, cyanobacteria, transport protein
• Biological source: Trichodesmium erythraeum (strain IMS101)
• Total number of polymer chains: 2
• Total formula weight: 62506.83

Authors

Bisson, C.,Adams, N.B.P.,Polyviou, D.,Bibby, T.S.,Hunter, C.N.,Hitchcock, A. (deposition date: 2016-05-11, release date: 2017-11-29, Last modification date: 2024-01-10)

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 (1.95 Å)