Evidence map›Paper›PMID 35503214›Full record

ArticleActa crystallographica. Section D, Structural biology2022

Structural insights into choline-O-sulfatase reveal the molecular determinants for ligand binding.

Jose Antonio Gavira, Ana Cámara-Artigas, Jose Luis Neira, Jesús M Torres de Pinedo, Pilar Sánchez, Esperanza Ortega, Sergio Martinez-Rodríguez

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Acta crystallographica. Section D, Structural biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact, top 97% 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

0 citing papers in PubMed, 0 citations in OpenAlex.

No citing paper in PubMed yet.

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 4 institutions in 1 country.

Jose Antonio GaviraLaboratorio de Estudios Cristalográficos, CSIC, Armilla, 18100 Granada, Spain.ORCID 0000-0002-7386-6484
Ana Cámara-ArtigasDepartment of Chemistry and Physics, University of Almería, Agrifood Campus of International Excellence (ceiA3), Research Centre for Agricultural and Food Biotechnology (BITAL), Carretera de Sacramento s/n, Almería, 04120, Spain.
Jose Luis NeiraIDIBE, Universidad Miguel Hernández, 03202 Elche (Alicante), Spain.
Jesús M Torres de PinedoDepartamento de Bioquímica y Biología Molecular III e Inmunología, Universidad de Granada, 18071 Granada, Spain.
Pilar SánchezDepartamento de Bioquímica y Biología Molecular III e Inmunología, Universidad de Granada, 18071 Granada, Spain.
Esperanza OrtegaDepartamento de Bioquímica y Biología Molecular III e Inmunología, Universidad de Granada, 18071 Granada, Spain.
Sergio Martinez-RodríguezLaboratorio de Estudios Cristalográficos, CSIC, Armilla, 18100 Granada, Spain.ORCID 0000-0001-6675-1550
Universidad de Granada · ESConsejo Superior de Investigaciones Científicas · ESUniversitat de Miguel Hernández d'Elx · ESUniversity of Almería · ES

Funding

Agencia Estatal de Investigación PID2020-116261GB-I00Agencia Estatal de Investigación RTI2018-097991-B-I00Junta de Andalucía PY20-00149Junta de Andalucía UAL18-BIO-B005-BUniversidad de Granada PPJI2017-1
6 · The paper itself

Abstract

Choline-O-sulfatase (COSe; EC 3.1.6.6) is a member of the alkaline phosphatase (AP) superfamily, and its natural function is to hydrolyze choline-O-sulfate into choline and sulfate. Despite its natural function, the major interest in this enzyme resides in the landmark catalytic/substrate promiscuity of sulfatases, which has led to attention in the biotechnological field due to their potential in protein engineering. In this work, an in-depth structural analysis of wild-type Sinorhizobium (Ensifer) meliloti COSe (SmeCOSe) and its C54S active-site mutant is reported. The binding mode of this AP superfamily member to both products of the reaction (sulfate and choline) and to a substrate-like compound are shown for the first time. The structures further confirm the importance of the C-terminal extension of the enzyme in becoming part of the active site and participating in enzyme activity through dynamic intra-subunit and inter-subunit hydrogen bonds (Asn146

Indexed as

Sinorhizobium melilotiSulfatasesAlkaline PhosphataseBinding SitesCholineLigandsSubstrate SpecificitySulfatesAlkaline PhosphataseCholineLigandsSulfatasesSulfatesalkaline phosphatasescholineconformational gatingpromiscuitysulfatases

Identifiers

PMID35503214
PMCPMC9063841
OpenAlexW4224555034

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.