1SU4

Crystal structure of calcium ATPase with two bound calcium ions

Replaces:  1EUL

Summary for 1SU4

• Entry DOI: 10.2210/pdb1su4/pdb
• Related: 1IWO 1VFP
• NMR Information: BMRB: 5765
• Descriptor: Sarcoplasmic/endoplasmic reticulum calcium ATPase 1, CALCIUM ION, SODIUM ION, ... (4 entities in total)
• Functional Keywords: ion pump, membrane protein, p-type atpase, active transport, hydrolase
• Biological source: Oryctolagus cuniculus (rabbit)
• Cellular location: Endoplasmic reticulum membrane ; Multi-pass membrane protein : P04191
• Total number of polymer chains: 1
• Total formula weight: 109705.72

Authors

Toyoshima, C.,Nakasako, M.,Nomura, H.,Ogawa, H. (deposition date: 2004-03-26, release date: 2004-05-04, Last modification date: 2024-10-23)

Primary citation

Toyoshima, C.,Nakasako, M.,Nomura, H.,Ogawa, H.
Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 A resolution
Nature, 405:647-655, 2000

PubMed Abstract: 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 A resolution with two calcium ions bound in the transmembrane domain, which comprises ten alpha-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.

PubMed: 10864315
DOI: 10.1038/35015017

Experimental method

X-RAY DIFFRACTION (2.4 Å)