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由四氨合钴 -ATP诱导产生新亚基相互作用的钠钾 -ATP酶二维晶体阵列

Two-dimensional crystalline arrays of Na,K-ATPase with new subunit interactions induced by cobalt-tetrammine-ATP.

作者信息

Skriver E, Maunsbach A B, Hebert H, Scheiner-Bobis G, Schoner W

机构信息

Department of Cell Biology, University of Aarhus, Denmark.

出版信息

J Ultrastruct Mol Struct Res. 1989 Dec;102(3):189-95. doi: 10.1016/0889-1605(89)90013-x.

DOI:10.1016/0889-1605(89)90013-x
PMID:2561364
Abstract

Purified membrane-bound Na,K-ATPase incubated with cobalt-tetrammine-ATP [Co(NH3)4ATP], which is a stable MgATP complex analog, shows two new types of membrane crystals, a new p21 form and a p4 form. The building blocks of the crystalline arrays correspond to (alpha beta)2 dimers of the enzyme protein suggesting that alpha-alpha interaction may be important in the pumping process.

摘要

用钴四氨ATP[Co(NH₃)₄ATP](一种稳定的MgATP复合物类似物)孵育纯化的膜结合钠钾ATP酶,会出现两种新型膜晶体,一种新的p21形式和一种p4形式。晶体阵列的结构单元对应于酶蛋白的(αβ)₂二聚体,这表明α-α相互作用在泵浦过程中可能很重要。

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Two-dimensional crystalline arrays of Na,K-ATPase with new subunit interactions induced by cobalt-tetrammine-ATP.由四氨合钴 -ATP诱导产生新亚基相互作用的钠钾 -ATP酶二维晶体阵列
J Ultrastruct Mol Struct Res. 1989 Dec;102(3):189-95. doi: 10.1016/0889-1605(89)90013-x.
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Three-dimensional structure of Na,K-ATPase determined from membrane crystals induced by cobalt-tetrammine-ATP.通过四氨合钴三磷酸腺苷诱导的膜晶体确定的钠钾-ATP酶的三维结构。
J Struct Biol. 1992 Mar-Apr;108(2):176-85. doi: 10.1016/1047-8477(92)90017-5.
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Demonstration of cooperating alpha subunits in working (Na+ + K+)-ATPase by the use of the MgATP complex analogue cobalt tetrammine ATP.利用MgATP复合类似物四氨合钴ATP证明工作中的(Na⁺ + K⁺)-ATP酶中协同作用的α亚基。
Eur J Biochem. 1987 Oct 1;168(1):123-31. doi: 10.1111/j.1432-1033.1987.tb13396.x.
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Phosphate binding and ATP-binding sites coexist in Na+/K(+)-transporting ATPase, as demonstrated by the inactivating MgPO4 complex analogue Co(NH3)4PO4.正如失活的MgPO4复合类似物Co(NH3)4PO4所证明的那样,磷酸结合位点和ATP结合位点共存于Na+/K(+)-转运ATP酶中。
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Shift to the Na+ form of Na+/K+-transporting ATPase due to modification of the low-affinity ATP-binding site by Co(NH3)4ATP.由于Co(NH₃)₄ATP对低亲和力ATP结合位点的修饰,Na⁺/K⁺转运ATP酶转变为Na⁺形式。
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How do MgATP analogues differentially modify high-affinity and low-affinity ATP binding sites of Na+/K(+)-ATPase?镁-三磷酸腺苷(MgATP)类似物如何差异性地修饰钠钾-三磷酸腺苷酶(Na+/K(+)-ATPase)的高亲和力和低亲和力三磷酸腺苷(ATP)结合位点?
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Modification of the E1ATP binding site of Na+/K(+)-ATPase by the chromium complex of adenosine 5'-[beta,gamma-methylene]triphosphate blocks the overall reaction but not the partial activities of the E2 conformation.腺苷5'-[β,γ-亚甲基]三磷酸的铬配合物对Na⁺/K⁺-ATP酶的E1ATP结合位点的修饰会阻断整个反应,但不会阻断E2构象的部分活性。
Eur J Biochem. 1993 Apr 15;213(2):743-8. doi: 10.1111/j.1432-1033.1993.tb17815.x.
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Inactivation of Na,K-ATPase following Co(NH3)4ATP binding at a low affinity site in the protomeric enzyme unit.在原聚体酶单位的低亲和力位点结合Co(NH3)4ATP后,钠钾ATP酶失活。
J Biol Chem. 2003 Apr 25;278(17):14688-97. doi: 10.1074/jbc.M211128200. Epub 2003 Feb 18.
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Binding of the Co(NH3)4 derivative of (2')3'-O-[N-methyl-anthraniloyl]-ATP to the E2ATP site of Na+/K+-transporting ATPase lowers the conformational flexibility of its E1ATP site.(2')3'-O-[N-甲基-邻氨基苯甲酰基]-ATP的Co(NH₃)₄衍生物与Na⁺/K⁺转运ATP酶的E2ATP位点结合会降低其E1ATP位点的构象灵活性。
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