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
相关论文
共 50 条
  • [21] STOICHIOMETRY OF PROTON TRANSPORT TO ATP HYDROLYSIS OF GASTRIC ATPASE
    REENSTRA, W
    FORTE, JG
    FEDERATION PROCEEDINGS, 1980, 39 (06) : 1966 - 1966
  • [22] Evidence for tryptophan residues in the cation transport path of the Na+,K+-ATPase
    Yudowski, GA
    Bar Shimon, M
    Tal, DM
    González-Lebrero, RM
    Rossi, RC
    Garrahan, PJ
    Beaugé, LA
    Karlish, SJD
    BIOCHEMISTRY, 2003, 42 (34) : 10212 - 10222
  • [23] ACTIVE CATION-TRANSPORT AND NA+K+MG ATPASE OF THE MONOTREME ERYTHROCYTES
    KIM, HD
    BAIRD, M
    SALLIS, J
    NICOL, S
    ISAACKS, RE
    BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 1984, 119 (03) : 1161 - 1167
  • [24] INTERACTION OF NA+,K+ AND ATP WITH NA,K-ATPASE
    GARRAHAN, PJ
    ROSSI, R
    REGA, AF
    CURRENT TOPICS IN MEMBRANES AND TRANSPORT, 1983, 19 : 561 - 564
  • [25] ACTIVE CATION TRANSPORT AND ATP HYDROLYSIS IN ACANTHAMOEBA SP
    KLEIN, RL
    BRELAND, AP
    COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY, 1966, 17 (01): : 39 - &
  • [26] Glucose regulation of pre-steady state kinetics of ATP hydrolysis by Na,K-ATPase
    Haque, Mohammad Mahfuzul
    Manzoor, Nikhat
    Amin, Mohammad
    Hussain, Mohammad Ejaz
    Khan, Luqman Ahmad
    ACTA BIOCHIMICA ET BIOPHYSICA SINICA, 2007, 39 (08) : 583 - 590
  • [27] Interaction region between catalytic subunits during ATP hydrolysis in oligomeric Na/K-ATPase.
    Kaya, S
    Imagawa, T
    Sakaguchi, K
    Taniguchi, K
    JOURNAL OF GENERAL PHYSIOLOGY, 2005, 126 (01): : 37A - 38A
  • [28] EVIDENCE FOR PARALLEL PATHWAYS OF PHOSPHOENZYME FORMATION IN THE MECHANISM OF ATP HYDROLYSIS BY ELECTROPHORUS NA,K-ATPASE
    FROEHLICH, JP
    HOBBS, AS
    ALBERS, RW
    CURRENT TOPICS IN MEMBRANES AND TRANSPORT, 1983, 19 : 513 - 535
  • [30] VOLUME CHANGES ASSOCIATED WITH HYDROLYSIS OF ATP BY TELEOST BRANCHIAL (NA+ + K+)-ATPASE AND MG2+-ATPASE
    PFEILER, E
    JOURNAL OF EXPERIMENTAL ZOOLOGY, 1980, 212 (02): : 291 - 299