3TLM
Crystal Structure of Endoplasmic Reticulum Ca2+-ATPase (SERCA) From Bovine Muscle
Summary for 3TLM
| Entry DOI | 10.2210/pdb3tlm/pdb |
| Related | 1SU4 1T5S |
| Descriptor | Sarcoplasmic/endoplasmic reticulum calcium ATPase 1, CALCIUM ION, MAGNESIUM ION, ... (6 entities in total) |
| Functional Keywords | serca, ca-atpase, calcium transporter, ca, fast-twitch muscle, hydrolase |
| Biological source | Bos taurus (bovine,cow,domestic cattle,domestic cow) |
| Cellular location | Endoplasmic reticulum membrane; Multi-pass membrane protein: Q0VCY0 |
| Total number of polymer chains | 1 |
| Total formula weight | 109995.06 |
| Authors | Sacchetto, R.,Bertipaglia, I.,Giannetti, S.,Cendron, L.,Mascarello, F.,Damiani, E.,Carafoli, E.,Zanotti, G. (deposition date: 2011-08-30, release date: 2012-03-21, Last modification date: 2023-09-13) |
| Primary citation | Sacchetto, R.,Bertipaglia, I.,Giannetti, S.,Cendron, L.,Mascarello, F.,Damiani, E.,Carafoli, E.,Zanotti, G. Crystal structure of sarcoplasmic reticulum Ca(2+)-ATPase (SERCA) from bovine muscle. J.Struct.Biol., 178:38-44, 2012 Cited by PubMed Abstract: The SERCA pump, a membrane protein of about 110kDa, transports two Ca(2+) ions per ATP hydrolyzed from the cytoplasm to the lumen of the sarcoplasmic reticulum. In muscle cells, its ability to remove Ca(2+) from the cytosol induces relaxation. The transport mechanism employed by the enzyme from rabbit muscle has been extensively studied, and several crystal structures representing different conformational states are available. However, no structure of the pump from other sources is known. In this paper we describe the crystal structure of the bovine enzyme, crystallized in the E1 conformation and determined at 2.9Å resolution. The overall molecular model is very similar to that of the rabbit enzyme, as expected by the high amino acid sequence identity. Nevertheless, the bovine enzyme has reduced catalytic activity with respect to the rabbit enzyme. Subtle structural modifications, in particular in the region of the long loop that protrudes into the SR lumen connecting transmembrane α-helices M7 and M8, may explain the difference. PubMed: 22387132DOI: 10.1016/j.jsb.2012.02.008 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.95 Å) |
Structure validation
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