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Cation transport coupled to ATP hydrolysis by the (Na, K)‐ATPase
Author(s) -
Leone Francisco A.,
Furriel Rosa P. M.,
McNamara John C.,
Horisberger Jean D.,
Borin Ivana A.
Publication year - 2010
Publication title -
biochemistry and molecular biology education
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.34
H-Index - 39
eISSN - 1539-3429
pISSN - 1470-8175
DOI - 10.1002/bmb.20404
Subject(s) - atp hydrolysis , atpase , hydrolysis , chemistry , biophysics , biochemistry , enzyme , biology
An Adobe® 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 α‐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.