Cation Transport Coupled to ATP Hydrolysis By the (Na, K)-ATPase AN INTEGRATED, ANIMATED MODEL

被引:3
|
作者
Leone, Francisco A. [1 ]
Furriel, Rosa P. M. [1 ]
McNamara, John C. [2 ]
Horisberger, Jean D. [1 ,3 ]
Borin, Ivana A. [1 ]
机构
[1] Univ Sao Paulo, Fac Filosofia Ciencias & Letras Ribeirao Preto, Dept Quim, BR-14040901 Sao Paulo, Brazil
[2] Univ Sao Paulo, Fac Filosofia Ciencias & Letras Ribeirao Preto, Dept Biol, BR-14040901 Sao Paulo, Brazil
[3] Univ Lausanne, Dept Pharmacol & Toxicol, Lausanne, Switzerland
基金
巴西圣保罗研究基金会;
关键词
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; CRYSTAL-STRUCTURE; SARCOPLASMIC-RETICULUM; BINDING-SITES; NA; K-ATPASE; MECHANISM; H;
D O I
10.1002/bmb.20404
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:276 / 279
页数:4
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