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


Journal

Acta crystallographica. Section D, Structural biology
ISSN: 2059-7983
Titre abrégé: Acta Crystallogr D Struct Biol
Pays: United States
ID NLM: 101676043

Informations de publication

Date de publication:
01 May 2022
Historique:
received: 13 12 2021
accepted: 04 04 2022
entrez: 3 5 2022
pubmed: 4 5 2022
medline: 6 5 2022
Statut: ppublish

Résumé

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

Identifiants

pubmed: 35503214
pii: S2059798322003709
doi: 10.1107/S2059798322003709
pmc: PMC9063841
doi:

Substances chimiques

Ligands 0
Sulfates 0
Alkaline Phosphatase EC 3.1.3.1
Sulfatases EC 3.1.6.-
Choline N91BDP6H0X

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

669-682

Subventions

Organisme : Agencia Estatal de Investigación
ID : PID2020-116261GB-I00
Organisme : Agencia Estatal de Investigación
ID : RTI2018-097991-B-I00
Organisme : Junta de Andalucía
ID : PY20-00149
Organisme : Junta de Andalucía
ID : UAL18-BIO-B005-B
Organisme : Universidad de Granada
ID : PPJI2017-1

Informations de copyright

open access.

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Auteurs

Jose Antonio Gavira (JA)

Laboratorio de Estudios Cristalográficos, CSIC, Armilla, 18100 Granada, Spain.

Ana Cámara-Artigas (A)

Department 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 Neira (JL)

IDIBE, Universidad Miguel Hernández, 03202 Elche (Alicante), Spain.

Jesús M Torres de Pinedo (JM)

Departamento de Bioquímica y Biología Molecular III e Inmunología, Universidad de Granada, 18071 Granada, Spain.

Pilar Sánchez (P)

Departamento de Bioquímica y Biología Molecular III e Inmunología, Universidad de Granada, 18071 Granada, Spain.

Esperanza Ortega (E)

Departamento de Bioquímica y Biología Molecular III e Inmunología, Universidad de Granada, 18071 Granada, Spain.

Sergio Martinez-Rodríguez (S)

Laboratorio de Estudios Cristalográficos, CSIC, Armilla, 18100 Granada, Spain.

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