Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 Å resolution

Chikashi Toyoshima, Masayoshi Nakasako, Hiromi Nomura, Haruo Ogawa

Research output: Contribution to journalArticlepeer-review

1610 Citations (Scopus)


Calcium ATPase is a member of the P-type ATPases that transport ions across the membrane against a concentration gradient. Here we have solved the crystal structure of the calcium ATPase of skeletal muscle sarcoplasmic reticulum (SERCA1a) at 2.6 Å resolution with two calcium ions bound in the transmembrane domain, which comprises ten α-helices. The two calcium ions are located side by side and are surrounded by four transmembrane helices, two of which are unwound for efficient coordination geometry. The cytoplasmic region consists of three well separated domains, with the phosphorylation site in the central catalytic domain and the adenosine-binding site on another domain. The phosphorylation domain has the same fold as haloacid dehalogenase. Comparison with a low-resolution electron density map of the enzyme in the absence of calcium and with biochemical data suggests that large domain movements take place during active transport.

Original languageEnglish
Pages (from-to)647-655
Number of pages9
Issue number6787
Publication statusPublished - 2000 Jun 8
Externally publishedYes

ASJC Scopus subject areas

  • General


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