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Structure, transmembrane topology and helix packing of P‐type ion pumps
Author(s) -
Stokes David L.,
Taylor William R.,
Green N.Michael
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)00297-5
Subject(s) - transmembrane domain , transmembrane protein , topology (electrical circuits) , helix (gastropod) , domain (mathematical analysis) , chemistry , biophysics , membrane topology , crystallography , membrane , biology , biochemistry , mathematics , combinatorics , ecology , mathematical analysis , receptor , snail
Electron microscopy has recently provided improved structures for P‐type ion pumps. In the case of Ca 2+ ‐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 Ca 2+ ‐ATPase. Thus, we present the most detailed model for transmembrane structure so far, in the hope of stimulating more precise experimental strategies.