Development of a structure determination method using a multidrug-resistance regulator protein as a framework.
Crystalline sponge method
Framework
In-house X-ray system
Multisite binding pocket
RamR
X-ray crystal structure
Journal
Biochemical and biophysical research communications
ISSN: 1090-2104
Titre abrégé: Biochem Biophys Res Commun
Pays: United States
ID NLM: 0372516
Informations de publication
Date de publication:
15 10 2019
15 10 2019
Historique:
received:
09
08
2019
accepted:
12
08
2019
pubmed:
23
8
2019
medline:
23
6
2020
entrez:
22
8
2019
Statut:
ppublish
Résumé
The structure determination of organic compounds is desirable for the development of medicines, aroma chemicals, and agricultural chemicals. However, the crystallization of organic compounds is often troublesome, because crystallization requires a relatively large quantity of high purity compounds and crystallization trials often need to be performed repetitively using different conditions. Some proteins are known to be able to bind to various organic compounds. The multidrug-resistance regulator protein RamR is one such protein. We have developed a structure determination method for organic compounds using RamR. RamR bound to organic compounds, including one compound that was not a known ligand for RamR, and the structures of the complexes were successfully determined. Because the RamR crystal is hydrophilic, this method may be useful for compounds that cannot be handled by the crystalline sponge method.
Identifiants
pubmed: 31431261
pii: S0006-291X(19)31587-6
doi: 10.1016/j.bbrc.2019.08.070
pii:
doi:
Substances chimiques
Ligands
0
Metal-Organic Frameworks
0
Multidrug Resistance-Associated Proteins
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
402-408Informations de copyright
Copyright © 2019 Elsevier Inc. All rights reserved.