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

Details

Serval ID
serval:BIB_DF29094AB7AB
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
Cation Transport Coupled to ATP Hydrolysis By the (Na, K)-ATPase : an integrated, animated model
Journal
Biochemistry and Molecular Biology Education
Author(s)
Leone Francisco A., Furriel Rosa P. M., McNamara John C., Horisberger Jean D., Borin Ivana A.
ISSN
1470-8175
Publication state
Published
Issued date
2010
Volume
38
Number
4
Pages
276-279
Language
english
Abstract
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.
Keywords
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
Yes
Create date
14/09/2010 13:23
Last modification date
20/10/2020 14:41
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