Phosphate-binding protein

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Function

Phosphate-binding protein (PBP) binds phosphate (Pi) with high affinity. PBP is involved in various biological processes like cell cycle regulation. PBP is produced under conditions of low Pi concentration. It binds Pi in the periplasm and transfers it to a membrane protein which transports it to the cytoplasm. PBP undergoes conformational change upon binding to Pi[1].

Structural highlights

The is highly selective. It can bind monobasic and dibasic phosphate but does not bind sulfate[2].

E. coli phosphate-binding protein complex with phosphate 1pbp

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3D structures of phosphate-binding protein3D structures of phosphate-binding protein

Updated on 22-September-2020

2v3q – hPBP + Pi – human
1qui, 1oib - EcPBP (mutant) - Escherichia coli
1pbp, 2abh, 1ixh – EcPBP + Pi
1qui - EcPBP (mutant) + Br + Pi
1quj, 1qul - EcPBP (mutant) + Cl + Pi
1quk, 1ixi, 1ixg, 1a40 - EcPBP (mutant) + Pi
1a54, 1a55 - EcPBP (mutant) + dihydrogenphosphate
1pc3, 4lvq – PBP + Pi – Mycobacterium tuberculosis
3w9v, 3w9w – upPBP + Pi – unidentified prokaryote
4m1v - upPBP (mutant) + Pi
4exl, 4h1x – SpPBP – Streptococcus pneumoniae
4lat – SpPBP + Pi
4omb, 4pqj – PBP + Pi – Pseudomonas aeruginosa
5wnn – PBP + Pi – Brucella melitensis
5ub3 – XcPBP – Xanthomonas citri
5i84, 5ub4 – XcPBP + Pi
5ub6 – XcPBP + PPi
5ub7 – XcPBP + ATP
5j1d – PBP + Pi – Stenotrophomonas maltophilia
4jwo – PBP – Planctomyces limnophilus

ReferencesReferences

  1. Gonzalez D, Richez M, Bergonzi C, Chabriere E, Elias M. Crystal structure of the phosphate-binding protein (PBP-1) of an ABC-type phosphate transporter from Clostridium perfringens. Sci Rep. 2014 Oct 16;4:6636. doi: 10.1038/srep06636. PMID:25338617 doi:http://dx.doi.org/10.1038/srep06636
  2. Wang Z, Choudhary A, Ledvina PS, Quiocho FA. Fine tuning the specificity of the periplasmic phosphate transport receptor. Site-directed mutagenesis, ligand binding, and crystallographic studies. J Biol Chem. 1994 Oct 7;269(40):25091-4. PMID:7929197

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Michal Harel, Alexander Berchansky, Joel L. Sussman