5lq8
From Proteopedia
1.52 A resolution structure of PhnD1 from Prochlorococcus marinus (MIT 9301) in complex with methylphosphonate
Structural highlights
FunctionPHND1_PROM0 Probably part of the ABC transporter complex PhnD1C1E1. Binds strongly to inorganic phosphite and with very weak affinities to methylphosphonate (MPn) and phosphate.[1] Publication Abstract from PubMedInorganic 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...pi 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. The molecular basis of phosphite and hypophosphite recognition by ABC-transporters.,Bisson C, Adams NBP, Stevenson B, Brindley AA, Polyviou D, Bibby TS, Baker PJ, Hunter CN, Hitchcock A Nat Commun. 2017 Nov 23;8(1):1746. doi: 10.1038/s41467-017-01226-8. PMID:29170493[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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