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5LQ5

1.46 A resolution structure of PhnD1 from Prochlorococcus marinus (MIT 9301) in complex with phosphite

Summary for 5LQ5
Entry DOI10.2210/pdb5lq5/pdb
Related5JVB 5LQ1
DescriptorPutative phosphonate binding protein for ABC transporter, PHOSPHITE ION (3 entities in total)
Functional Keywordsabc-transporter, phosphite, prochlorococcus, periplasmic binding protein, transport protein
Biological sourceProchlorococcus marinus str. MIT 9301
Cellular locationPeriplasm : A3PC74
Total number of polymer chains1
Total formula weight32408.02
Authors
Bisson, C.,Adams, N.B.P.,Polyviou, D.,Bibby, T.S.,Hunter, C.N.,Hitchcock, A. (deposition date: 2016-08-16, release date: 2017-12-06, Last modification date: 2024-01-10)
Primary citationBisson, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.46 Å)
Structure validation

227344

数据于2024-11-13公开中

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