5LQ8

1.52 A resolution structure of PhnD1 from Prochlorococcus marinus (MIT 9301) in complex with methylphosphonate

5LQ8 の概要

• エントリーDOI: 10.2210/pdb5lq8/pdb
• 関連するPDBエントリー: 5JVB 5LQ1 5LQ5
• 分子名称: Putative phosphonate binding protein for ABC transporter, METHYLPHOSPHONIC ACID ESTER GROUP (3 entities in total)
• 機能のキーワード: abc-transporter, methylphosphonate, prochlorococcus, periplasmic binding protein
• 由来する生物種: Prochlorococcus marinus str. MIT 9301
• 細胞内の位置: Periplasm : A3PC74
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 32521.09

構造登録者

Bisson, C.,Adams, N.B.P.,Polyviou, D.,Bibby, T.S.,Hunter, C.N.,Hitchcock, A. (登録日: 2016-08-16, 公開日: 2017-12-06, 最終更新日: 2024-01-10)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.52 Å)