Phosphate-binding protein
From Proteopedia
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== Function == | == 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<ref>PMID:25338617</ref>. | '''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<ref>PMID:25338617</ref>. | ||
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== Structural highlights == | == Structural highlights == | ||
The PBP phosphate-binding site is highly selective. It can bind monobasic and dibasic phosphate but does not bind sulfate<ref>PMID:7929197</ref>. | The PBP phosphate-binding site is highly selective. It can bind monobasic and dibasic phosphate but does not bind sulfate<ref>PMID:7929197</ref>. | ||
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==3D structures of phosphate-binding protein== | ==3D structures of phosphate-binding protein== | ||
Revision as of 08:44, 8 September 2016
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3D structures of phosphate-binding protein
Updated on 08-September-2016
1qui, 1oib - EcPBP (mutant) - Escherichia coli
4jwo – PBP – Planctomyces limnophilus
4exl, 4h1x – SpPBP – Streptococcus pneumoniae
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
2v3q – hPBP + Pi – human
1pc3, 4lvq – PBP + Pi – Mycobacterium tuberculosis
3w9v, 3w9w – upPBP + Pi – unidentified prokaryote
4lat – SpPBP + Pi
4m1v - upPBP (mutant) + Pi
4omb, 4pqj – PBP + Pi – Pseudomonas aeruginosa
References
- ↑ 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
- ↑ 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
