Evidence map›Paper›PMID 28580922›Full record

ArticleActa crystallographica. Section F, Structural biology communications2017

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

Vanessa R Pegos, Louis Hey, Jacob LaMirande, Rachel Pfeffer, Rosalie Lipsh, Moshe Amitay, Daniel Gonzalez, Mikael Elias

Abstract read
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In one paragraph

Article in Acta crystallographica. Section F, Structural biology communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

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3 · Its place in the literature

Who cites it

1 citing paper in PubMed.

  1. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors.

Vanessa R PegosBiochemistry, Molecular Biology and Biophysics Department and BioTechnology Institute, University of Minnesota, Saint Paul, MN 55108, USA.
Louis HeyBiochemistry, Molecular Biology and Biophysics Department and BioTechnology Institute, University of Minnesota, Saint Paul, MN 55108, USA.
Jacob LaMirandeBiochemistry, Molecular Biology and Biophysics Department and BioTechnology Institute, University of Minnesota, Saint Paul, MN 55108, USA.
Rachel PfefferDepartment of Bioinformatics, The Jerusalem College of Technology - Lev Academic Center, Jerusalem 91160, Israel.
Rosalie LipshDepartment of Bioinformatics, The Jerusalem College of Technology - Lev Academic Center, Jerusalem 91160, Israel.
Moshe AmitayDepartment of Bioinformatics, The Jerusalem College of Technology - Lev Academic Center, Jerusalem 91160, Israel.
Daniel GonzalezURMITE, Aix Marseille Université, INSERM, CNRS, IRD, 27 Boulevard Jean Moulin, 13385 Marseille, France.
Mikael EliasBiochemistry, Molecular Biology and Biophysics Department and BioTechnology Institute, University of Minnesota, Saint Paul, MN 55108, USA.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

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 from Polaromonas JS666 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 from Polaromonas JS666 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 from Polaromonas JS666 are reported.

Indexed as

Amino Acid SequenceBacterial ProteinsCloning, MolecularComamonadaceaeCrystallizationCrystallography, X-RayEscherichia coliGene ExpressionGenetic VectorsHydrogen BondingHydrogen-Ion ConcentrationPeriplasmPhosphate-Binding ProteinsPhosphatesRecombinant Fusion ProteinsSequence AlignmentBacterial ProteinsPhosphate-Binding ProteinsPhosphatesRecombinant Fusion Proteinsmolecular specificityphosphate ABC transporterphosphate-binding proteinPolaromonas JS666

Identifiers

PMID28580922
PMCPMC5458391

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.