Cis-trans proline isomers in the catalytic domain of calcineurin.
NMR
13C-methyl methionine NMR
calcineurin
cis-trans isomerization
phosphatase
Journal
The FEBS journal
ISSN: 1742-4658
Titre abrégé: FEBS J
Pays: England
ID NLM: 101229646
Informations de publication
Date de publication:
03 2019
03 2019
Historique:
received:
23
07
2018
revised:
06
11
2018
accepted:
03
12
2018
pubmed:
12
12
2018
medline:
1
5
2020
entrez:
12
12
2018
Statut:
ppublish
Résumé
Calcineurin is an essential calcium-activated serine/threonine phosphatase. The six NMR-observable methionine methyl groups in the catalytic domain of human calcineurin Aα (CNA) were assigned and used as reporters of the presence of potential cis-trans isomers in solution. Proline 84 is found in the cis conformation in most calcineurin X-ray structures, and proline 309, which is part of a highly conserved motif in phosphoprotein phosphatases, was modeled with a cis peptide bond in one of the two molecules present in the asymmetric unit of CNA. We mutated each of the two prolines to alanine to force the trans conformation. Solution NMR shows that the P84A CNA mutant exists in two forms, compatible with cis-trans isomers, while the P309A mutant is predominantly in the trans conformation. DATABASE: PDB depositions mentioned PDB 5C1V and 2JOG.
Substances chimiques
Proline
9DLQ4CIU6V
Methionine
AE28F7PNPL
Calcineurin
EC 3.1.3.16
PPP3CA protein, human
EC 3.1.3.16
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
1230-1239Informations de copyright
© 2018 Federation of European Biochemical Societies.