Evidence map›Paper›PMID 23034649›Full record

ArticleNature2012

The molecular basis of phosphate discrimination in arsenate-rich environments.

Mikael Elias, Alon Wellner, Korina Goldin-Azulay, Eric Chabriere, Julia A Vorholt, Tobias J Erb, Dan S Tawfik

Abstract read
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In one paragraph

Article in Nature, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 75 papers.

0numbers the graph read from it
0cells of the map it votes in
75citing papers in PubMed
12.2field-weighted citation impact, top 1% of its field
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

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

75 citing papers in PubMed, 217 citations in OpenAlex.

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  15. Are cysteine, glutathione and phytochelatins responses of Myriophyllum alterniflorum to copper and arsenic stress affected by trophic conditions?Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2022
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15 more citing papers are in PubMed but not listed here.

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

7 authors at 3 institutions in 3 countries.

Mikael EliasDepartment of Biological Chemistry, Weizmann Institute of Science, Rehovot 76100, Israel. mikael.elias@weizmann.ac.il
Alon Wellner
Korina Goldin-Azulay
Eric Chabriere
Julia A Vorholt
Tobias J Erb
Dan S Tawfik
Weizmann Institute of Science · ILBoard of the Swiss Federal Institutes of Technology · CHCentre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Arsenate and phosphate are abundant on Earth and have striking similarities: nearly identical pK(a) values, similarly charged oxygen atoms, and thermochemical radii that differ by only 4% (ref. 3). Phosphate is indispensable and arsenate is toxic, but this extensive similarity raises the question whether arsenate may substitute for phosphate in certain niches. However, whether it is used or excluded, discriminating phosphate from arsenate is a paramount challenge. Enzymes that utilize phosphate, for example, have the same binding mode and kinetic parameters as arsenate, and the latter's presence therefore decouples metabolism. Can proteins discriminate between these two anions, and how would they do so? In particular, cellular phosphate uptake systems face a challenge in arsenate-rich environments. Here we describe a molecular mechanism for this process. We examined the periplasmic phosphate-binding proteins (PBPs) of the ABC-type transport system that mediates phosphate uptake into bacterial cells, including two PBPs from the arsenate-rich Mono Lake Halomonas strain GFAJ-1. All PBPs tested are capable of discriminating phosphate over arsenate at least 500-fold. The exception is one of the PBPs of GFAJ-1 that shows roughly 4,500-fold discrimination and its gene is highly expressed under phosphate-limiting conditions. Sub-ångström-resolution structures of Pseudomonas fluorescens PBP with both arsenate and phosphate show a unique mode of binding that mediates discrimination. An extensive network of dipole-anion interactions, and of repulsive interactions, results in the 4% larger arsenate distorting a unique low-barrier hydrogen bond. These features enable the phosphate transport system to bind phosphate selectively over arsenate (at least 10(3) excess) even in highly arsenate-rich environments.

Indexed as

Adenosine TriphosphateArsenatesBinding SitesBiological TransportCrystallography, X-RayDrug Resistance, BacterialEcosystemEscherichia coliHydrogen BondingLakesModels, MolecularPeriplasmic Binding ProteinsPhosphate-Binding ProteinsPhosphatesPseudomonas fluorescensSubstrate SpecificityAdenosine TriphosphateArsenatesarsenic acidPeriplasmic Binding ProteinsPhosphate-Binding ProteinsPhosphates

Identifiers

PMID23034649
OpenAlexW2071298877

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.