Cation Transport Coupled to ATP Hydrolysis By the (Na, K)-ATPase : an integrated, animated model

Détails

ID Serval
serval:BIB_DF29094AB7AB
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
Cation Transport Coupled to ATP Hydrolysis By the (Na, K)-ATPase : an integrated, animated model
Périodique
Biochemistry and Molecular Biology Education
Auteur(s)
Leone Francisco A., Furriel Rosa P. M., McNamara John C., Horisberger Jean D., Borin Ivana A.
ISSN
1470-8175
Statut éditorial
Publié
Date de publication
2010
Volume
38
Numéro
4
Pages
276-279
Langue
anglais
Résumé
An Adobe (R) animation is presented for use in undergraduate Biochemistry courses, illustrating the mechanism of Na+ and K+ translocation coupled to ATP hydrolysis by the (Na, K)-ATPase, a P-2c-type ATPase, or ATP-powered ion pump that actively translocates cations across plasma membranes. The enzyme is also known as an E-1/E-2-ATPase as it undergoes conformational changes between the E-1 and E-2 forms during the pumping cycle, altering the affinity and accessibility of the transmembrane ion-binding sites. The animation is based on Horisberger's scheme that incorporates the most recent significant findings to have improved our understanding of the (Na, K)-ATPase structure function relationship. The movements of the various domains within the (Na, K)-ATPase alpha-subunit illustrate the conformational changes that occur during Na+ and K+ translocation across the membrane and emphasize involvement of the actuator, nucleotide, and phosphorylation domains, that is, the "core engine" of the pump, with respect to ATP binding, cation transport, and ADP and P-i release.
Mots-clé
enzymes and catalysis, original models for teaching and learning, transport through membranes, using multimedia in the classroom, SODIUM-POTASSIUM PUMP, P-TYPE ATPASES, CALCIUM-PUMP, SARCOPLASMIC-RETICULUM, CRYSTAL-STRUCTURE, BINDING-SITES, NA,K-ATPASE, MECHANISM, H,K-ATPASE
Web of science
Open Access
Oui
Création de la notice
14/09/2010 14:23
Dernière modification de la notice
20/10/2020 15:41
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