Structural basis for the counter-transport mechanism of a H +/Ca2+ exchanger

Tomohiro Nishizawa, Satomi Kita, Andrés D. Maturana, Noritaka Furuya, Kunio Hirata, Go Kasuya, Satoshi Ogasawara, Naoshi Dohmae, Takahiro Iwamoto, Ryuichiro Ishitani, Osamu Nureki

Research output: Contribution to journalArticle

45 Citations (Scopus)

Abstract

Ca2+/cation antiporters catalyze the exchange of Ca2+ with various cations across biological membranes to regulate cytosolic calcium levels. The recently reported structure of a prokaryotic Na+/Ca 2+ exchanger (NCX-Mj) revealed its overall architecture in an outward-facing state. Here, we report the crystal structure of a H +/Ca2+ exchanger from Archaeoglobus fulgidus (CAX-Af) in the two representatives of the inward-facing conformation at 2.3 Å resolution. The structures suggested Ca2+ or H+ binds to the cation-binding site mutually exclusively. Structural comparison of CAX-Af with NCX-Mj revealed that the first and sixth transmembrane helices alternately create hydrophilic cavities on the intra- and extracellular sides. The structures and functional analyses provide insight into the mechanism of how the inward- to outward-facing state transition is triggered by the Ca2+ and H+ binding.

Original languageEnglish
Pages (from-to)168-172
Number of pages5
JournalScience
Volume341
Issue number6142
DOIs
Publication statusPublished - 2013 Jan 1

ASJC Scopus subject areas

  • Medicine(all)
  • General

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    Nishizawa, T., Kita, S., Maturana, A. D., Furuya, N., Hirata, K., Kasuya, G., Ogasawara, S., Dohmae, N., Iwamoto, T., Ishitani, R., & Nureki, O. (2013). Structural basis for the counter-transport mechanism of a H +/Ca2+ exchanger. Science, 341(6142), 168-172. https://doi.org/10.1126/science.1239002