The pi-helix formation between Asp369 and Thr375 as a key factor in E1-E2 conformational change of Na+/K+-ATPase
Language English Country Czech Republic Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
18657006
DOI
10.33549/physiolres.931469
PII: 1469
Knihovny.cz E-resources
- MeSH
- Kinetics MeSH
- Aspartic Acid chemistry genetics MeSH
- Models, Molecular MeSH
- Protein Isoforms chemistry metabolism MeSH
- Protein Structure, Secondary MeSH
- Sodium-Potassium-Exchanging ATPase chemistry genetics metabolism MeSH
- Threonine chemistry genetics MeSH
- Binding Sites MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Aspartic Acid MeSH
- Protein Isoforms MeSH
- Sodium-Potassium-Exchanging ATPase MeSH
- Threonine MeSH
Molecular modeling of the H4-H5-loop of the alpha2 isoform of Na+/K+-ATPase in the E1 and E2 conformations revealed that twisting of the nucleotide (N) domain toward the phosphorylation (P) domain is connected with the formation of a short pi-helix between Asp369 and Thr375. This conformational change close to the hinge region between the N-domain and the P-domain could be an important event leading to a bending of the N-domain by 64.7 degrees and to a shortening of the distance between the ATP binding site and the phosphorylation site (Asp369) by 1.22 nm from 3.22 nm to 2.00 nm. It is hypothesized that this shortening mechanism is involved in the Na+-dependent formation of the Asp369 phospho-intermediate as part of the overall Na+/K+-ATPase activity.
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