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Crystal structure of the SR Ca2+-ATPase in the Ca2-E1-MgAMPPCP form determined by serial femtosecond crystallography using an X-ray free-electron laser.Crystal structure of the SR Ca2+-ATPase in the Ca2-E1-MgAMPPCP form determined by serial femtosecond crystallography using an X-ray free-electron laser.
Structural highlights
Function[AT2A1_RABIT] This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen. Contributes to calcium sequestration involved in muscular excitation/contraction (By similarity). |
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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCACategories:
- Calcium-transporting ATPase
- Oryctolagus cuniculus
- Barends, T R.M
- Boesen, T
- Boutet, S
- Bublitz, M
- Clausen, J D
- Doak, R B
- Drachmann, N D
- Foucar, L
- Gotfryd, K
- Gregersen, J L
- Gutmann, M J
- Markvardsen, A J
- Mattle, D
- Messerschmidt, M
- Moller, J V
- Nass, K
- Nissen, P
- Olesen, C
- Reinhard, L
- Schlichting, I
- Seibert, M M
- Shoeman, R L
- Sitsel, O
- Wang, K T
- Williams, G J
- Hydrolase
- P-type atpase
- Serial femtosecond crystallography
- X-ray free electron laser