Homology Modeling of an Algal Membrane Protein, Heterosigma Akashiwo Na+–ATPase

Abstract

Original Contribution： MEMBRANE， 35（2） ，80 85（2010）The three-dimensional structure of Heterosigma akashiwo Na + -ATPase (HANA) was predicted by means of homology modeling based on the crystal structure of the K + -bound form of shark Na + /K + -ATPase (PDB ID: 2ZXE). The overall structure of HANA appears to be similar to that of shark Na + /K + -ATPase. Both contain three characteristic cytoplasmic domains, A, N and P, which are unique to P-type ATPases. HANA has a long TM7-8 junction as a large extracellular domain, in place of the β-subunit of shark Na + /K + -ATPase. Two putative K + -binding sites in the transmembrane domain of HANA were identified by means of valence mapping based on the constructed structure. The presence of K + -binding sites and the reported ion requirements for ATPase activity and EP formation indicate that HANA may transport K + ions in the same manner as animal Na + /K + -ATPases.

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