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Title: Phosphate-binding protein from Polaromonas JS666: purification, characterization, crystallization and sulfur SAD phasing

Abstract

Phosphate-binding proteins (PBPs) are key proteins that belong to the bacterial ABC-type phosphate transporters. PBPs are periplasmic (or membrane-anchored) proteins that capture phosphate anions from the environment and release them to the transmembrane transporter. Recent work has suggested that PBPs have evolved for high affinity as well as high selectivity. In particular, a short, unique hydrogen bond between the phosphate anion and an aspartate residue has been shown to be critical for selectivity, yet is not strictly conserved in PBPs. Here, the PBP fromPolaromonasJS666 is focused on. Interestingly, this PBP is predicted to harbor different phosphate-binding residues to currently known PBPs. Here, it is shown that the PBP fromPolaromonasJS666 is capable of binding phosphate, with a maximal binding activity at pH 8. Its structure is expected to reveal its binding-cleft configuration as well as its phosphate-binding mode. Here, the expression, purification, characterization, crystallization and X-ray diffraction data collection to 1.35 Å resolution of the PBP fromPolaromonasJS666 are reported.

Authors:
; ; ; ; ; ; ; ORCiD logo
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Org.:
UNIVERSITY
OSTI Identifier:
1373794
Resource Type:
Journal Article
Resource Relation:
Journal Name: Acta Crystallographica. Section F, Structural Biology Communications; Journal Volume: 73; Journal Issue: 6
Country of Publication:
United States
Language:
ENGLISH
Subject:
59 BASIC BIOLOGICAL SCIENCES

Citation Formats

Pegos, Vanessa R., Hey, Louis, LaMirande, Jacob, Pfeffer, Rachel, Lipsh, Rosalie, Amitay, Moshe, Gonzalez, Daniel, and Elias, Mikael. Phosphate-binding protein from Polaromonas JS666: purification, characterization, crystallization and sulfur SAD phasing. United States: N. p., 2017. Web. doi:10.1107/S2053230X17007373.
Pegos, Vanessa R., Hey, Louis, LaMirande, Jacob, Pfeffer, Rachel, Lipsh, Rosalie, Amitay, Moshe, Gonzalez, Daniel, & Elias, Mikael. Phosphate-binding protein from Polaromonas JS666: purification, characterization, crystallization and sulfur SAD phasing. United States. doi:10.1107/S2053230X17007373.
Pegos, Vanessa R., Hey, Louis, LaMirande, Jacob, Pfeffer, Rachel, Lipsh, Rosalie, Amitay, Moshe, Gonzalez, Daniel, and Elias, Mikael. Thu . "Phosphate-binding protein from Polaromonas JS666: purification, characterization, crystallization and sulfur SAD phasing". United States. doi:10.1107/S2053230X17007373.
@article{osti_1373794,
title = {Phosphate-binding protein from Polaromonas JS666: purification, characterization, crystallization and sulfur SAD phasing},
author = {Pegos, Vanessa R. and Hey, Louis and LaMirande, Jacob and Pfeffer, Rachel and Lipsh, Rosalie and Amitay, Moshe and Gonzalez, Daniel and Elias, Mikael},
abstractNote = {Phosphate-binding proteins (PBPs) are key proteins that belong to the bacterial ABC-type phosphate transporters. PBPs are periplasmic (or membrane-anchored) proteins that capture phosphate anions from the environment and release them to the transmembrane transporter. Recent work has suggested that PBPs have evolved for high affinity as well as high selectivity. In particular, a short, unique hydrogen bond between the phosphate anion and an aspartate residue has been shown to be critical for selectivity, yet is not strictly conserved in PBPs. Here, the PBP fromPolaromonasJS666 is focused on. Interestingly, this PBP is predicted to harbor different phosphate-binding residues to currently known PBPs. Here, it is shown that the PBP fromPolaromonasJS666 is capable of binding phosphate, with a maximal binding activity at pH 8. Its structure is expected to reveal its binding-cleft configuration as well as its phosphate-binding mode. Here, the expression, purification, characterization, crystallization and X-ray diffraction data collection to 1.35 Å resolution of the PBP fromPolaromonasJS666 are reported.},
doi = {10.1107/S2053230X17007373},
journal = {Acta Crystallographica. Section F, Structural Biology Communications},
number = 6,
volume = 73,
place = {United States},
year = {Thu May 25 00:00:00 EDT 2017},
month = {Thu May 25 00:00:00 EDT 2017}
}