Structure, transmembrane topology and helix packing of P‐type ion pumps

FEBS Letters

Taylor, William R.²  Green, N.Michael²  Stokes, David L.¹ 

[1] Department of Molecular Physiology and Biological Physics, Box 449, University of Virginia Health Sciences Center, Charlottesville, VA 22908, USA;Laboratory of Mathematical Biology, National Institute for Medical Research, Mill Hill, London NW7 1AA, UK

关键词: Ion transport;    Membrane domain;    Protein structure;    Protein folding;    Ca2+-ATPase;    Na+/K+-ATPase;   

DOI  :  10.1016/0014-5793(94)00297-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Electron microscopy has recently provided improved structures for P-type ion pumps. In the case of Ca²⁺-ATPase, the use of unstained specimens revealed the structure of the transmembrane domain. The composition of this domain has been controversial due to the variety of methods used to study the number and exact locations of transmembrane crossings within the sequence. After reviewing the results from several members of the family, we found a consensus for 10 transmembrane segments, and also that 10 helices fitted well into the structure of Ca²⁺-ATPase. Thus, we present the most detailed model for transmembrane structure so far, in the hope of stimulating more precise experimental strategies.

【 授权许可】

Unknown