Unraveling structural insights of ribokinase from Leishmania donovani.
Leishmania donovani
Nucleotide-binding site
Protein crystallography
Ribokinase
Substrate-binding pocket
Journal
International journal of biological macromolecules
ISSN: 1879-0003
Titre abrégé: Int J Biol Macromol
Pays: Netherlands
ID NLM: 7909578
Informations de publication
Date de publication:
01 Sep 2019
01 Sep 2019
Historique:
received:
15
03
2019
revised:
29
05
2019
accepted:
01
06
2019
pubmed:
7
6
2019
medline:
31
12
2019
entrez:
7
6
2019
Statut:
ppublish
Résumé
Ribokinase (RK) is an ATP dependent sugar kinase that enables the entry of ribose in the metabolism. Leishmania accumulates ribose into the cytosol through hydrolysis of nucleosides and by transport from the extracellular environment. Activation by RK is critical to mobilize the ribose into the metabolism of Leishmania. To understand the catalytic role, the crystal structure of RK (LdRK) from L. donovani was determined in the apo and complex forms with several nucleotides (ATP, AMPPCP and ADP) in the presence of Na
Identifiants
pubmed: 31170491
pii: S0141-8130(19)31946-4
doi: 10.1016/j.ijbiomac.2019.06.001
pii:
doi:
Substances chimiques
Nucleotides
0
Phosphates
0
Phosphotransferases (Alcohol Group Acceptor)
EC 2.7.1.-
ribokinase
EC 2.7.1.15
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
253-265Informations de copyright
Copyright © 2019. Published by Elsevier B.V.