Evidence map›Paper›PMID 35400670›Full record

ArticleActa crystallographica. Section F, Structural biology communications2022

The structure of Synechococcus elongatus enolase reveals key aspects of phosphoenolpyruvate binding.

Javier M González, Ricardo Martí-Arbona, Julian C H Chen, Clifford J Unkefer

Open access · hybridAbstract read
In one paragraph

Article in Acta crystallographica. Section F, Structural biology communications, 2022. 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
0.1field-weighted citation impact, top 65% 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

1 citing paper in PubMed, 2 citations in OpenAlex.

  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

4 authors at 2 institutions in 2 countries.

Javier M GonzálezInstituto de Bionanotecnología del NOA (INBIONATEC-CONICET), Universidad Nacional de Santiago del Estero (UNSE), RN9, Km1125, G4206XCP Santiago del Estero, Argentina.ORCID 0000-0002-3298-2235
Ricardo Martí-ArbonaBioscience Division, Los Alamos National Laboratory, Los Alamos, NM 87545, USA.ORCID 0000-0002-9720-977X
Julian C H ChenBioscience Division, Los Alamos National Laboratory, Los Alamos, NM 87545, USA.ORCID 0000-0003-0341-165X
Clifford J UnkeferBioscience Division, Los Alamos National Laboratory, Los Alamos, NM 87545, USA.ORCID 0000-0002-9263-3221
Los Alamos National Laboratory · USNational University of Santiago del Estero · AR

Funding

A Synchrotron Radiation Structural Biology ResourcesP30GM133894 · NIGMS · STANFORD UNIVERSITY · PI Ritimukta Sarangi · 2020 to 2026
$43.3M
Agencia Nacional de Promoción Científica y Tecnológica PICT2017-4590Los Alamos National Laboratory 20120776PRD4Los Alamos National Laboratory 20130091DRNIGMS NIH HHS P30 GM133894
6 · The paper itself

Abstract

A structure-function characterization of Synechococcus elongatus enolase (SeEN) is presented, representing the first structural report on a cyanobacterial enolase. X-ray crystal structures of SeEN in its apoenzyme form and in complex with phosphoenolpyruvate are reported at 2.05 and 2.30 Å resolution, respectively. SeEN displays the typical fold of enolases, with a conformationally flexible loop that closes the active site upon substrate binding, assisted by two metal ions that stabilize the negatively charged groups. The enzyme exhibits a catalytic efficiency of 1.2 × 10

Indexed as

Phosphopyruvate HydrataseSynechococcusCrystallography, X-RayPhosphoenolpyruvatePhosphoenolpyruvatePhosphopyruvate HydratasecyanobacteriaenolasesphosphoenolpyruvateSynechococcus elongatus

Identifiers

PMID35400670
PMCPMC8996150
OpenAlexW4223419017

What OpenQuestion holds

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LicenceCC BY
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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.