AI Article Synopsis
- The review focuses on the relationship between the structure and function of the M1 transmembrane segment in Na+,K+-ATPase and Ca2+-ATPase.
- The hypothesis that charged residues in the N-terminal part of M1 interact with transported cations is rejected, while hydrophobic residues in the middle of M1 are crucial for cation interaction.
- Specific residues, Leu65 in Ca2+-ATPase and Leu99 in Na+,K+-ATPase, act as gate-locking residues that influence cation dynamics, and a structural pivot in M1 and M3 is key for gate opening.
Article Abstract
In this review we summarize mutagenesis work on the structure-function relationship of transmembrane segment M1 in the Na+,K+-ATPase and the sarco(endo)plasmic reticulum Ca2+-ATPase. The original hypothesis that charged residues in the N-terminal part of M1 interact with the transported cations can be rejected. On the other hand hydrophobic residues in the middle part of M1 turned out to play crucial roles in Ca2+ interaction/occlusion in Ca2+-ATPase and K+ interaction/occlusion in Na+,K+-ATPase. Leu65 of the Ca2+-ATPase and Leu99 of the Na+,K+-ATPase, located at homologous positions in M1, function as gate-locking residues that restrict the mobility of the side chain of the cation binding/gating residue of transmembrane segment M4, Glu309/Glu329. A pivot formed between a pair of a glycine and a bulky residue in M1 and M3 seems critical to the opening of the extracytoplasmic gate in both the Ca2+-ATPase and the Na+,K+-ATPase.
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| http://dx.doi.org/10.1007/s10863-007-9106-x | DOI Listing |
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