Homology Modeling of an Algal Membrane Protein, Heterosigma Akashiwo Na+–ATPase
-
- Jo Taeho
- Biochemistry and Biophysics, Graduate School of Healthcare Sciences Tokyo Medical and Dental University
-
- Shono Mariko
- Tropical Agriculture Research Front, Japan International Research Center for Agricultural Sciences
-
- Wada Masato
- Apple Research Station, National Institute of Fruit Tree Science, National Agriculture and Food Research Organization
-
- Ito Sayaka
- Biochemistry and Biophysics, Graduate School of Healthcare Sciences Tokyo Medical and Dental University
-
- Nomoto Junko
- Biochemistry and Biophysics, Graduate School of Healthcare Sciences Tokyo Medical and Dental University
-
- Hara Yukichi
- Biochemistry and Biophysics, Graduate School of Healthcare Sciences Tokyo Medical and Dental University
Search this article
Abstract
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.
Journal
-
- MEMBRANE
-
MEMBRANE 35 (2), 80-85, 2010
THE MEMBRANE SOCIETY OF JAPAN
- Tweet
Details 詳細情報について
-
- CRID
- 1390001206421588480
-
- NII Article ID
- 130005075551
- 10026877117
-
- NII Book ID
- AN0023215X
-
- ISSN
- 18846440
- 03851036
-
- NDL BIB ID
- 10635083
-
- Text Lang
- en
-
- Data Source
-
- JaLC
- NDL
- Crossref
- CiNii Articles
-
- Abstract License Flag
- Disallowed