New structural insights provide a different angle on steroid sulfatase action.
Membrane-associated
Steroid sulfatase
Structural biology
Sulfation pathways
Trimer formation
Journal
The Journal of steroid biochemistry and molecular biology
ISSN: 1879-1220
Titre abrégé: J Steroid Biochem Mol Biol
Pays: England
ID NLM: 9015483
Informations de publication
Date de publication:
09 2023
09 2023
Historique:
received:
28
03
2023
revised:
08
06
2023
accepted:
16
06
2023
medline:
25
8
2023
pubmed:
19
6
2023
entrez:
18
6
2023
Statut:
ppublish
Résumé
A central part of human sulfation pathways is the spatially and temporally controlled desulfation of biologically highly potent steroid hormones. The responsible enzyme - steroid sulfatase (STS) - is highly expressed in placenta and peripheral tissues, such as fat, colon, and the brain. The shape of this enzyme and its mechanism are probably unique in biochemistry. STS was believed to be a transmembrane protein, spanning the Golgi double-membrane by stem region formed by two extended internal alpha-helices. New crystallographic data however challenge this view. STS now is portraited as a trimeric membrane-associated complex. We discuss the impact of these results on STS function and sulfation pathways in general and we hypothesis that this new STS structural understanding suggests product inhibition to be a regulator of STS enzymatic activity.
Identifiants
pubmed: 37331434
pii: S0960-0760(23)00108-5
doi: 10.1016/j.jsbmb.2023.106353
pii:
doi:
Substances chimiques
Steryl-Sulfatase
EC 3.1.6.2
Steroids
0
Membrane Proteins
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
106353Informations de copyright
Copyright © 2023 The Authors. Published by Elsevier Ltd.. All rights reserved.