5XAA
Complete structure factors and an atomic model of the calcium pump (SERCA1A) and associated phospholipids in the E2-ALF-(TG) crystals of P21212 symmetry
Summary for 5XAA
| Entry DOI | 10.2210/pdb5xaa/pdb |
| Related | 5XA7 5XA8 5XA9 5XAB |
| Descriptor | Sarcoplasmic/endoplasmic reticulum calcium ATPase 1, MAGNESIUM ION, TETRAFLUOROALUMINATE ION, ... (6 entities in total) |
| Functional Keywords | p-type atpase, hydrolase, calcium transport, calcium binding, atp binding, endoplasmic reticulum, sarcoplasmic reticulum, metal transport |
| Biological source | Oryctolagus cuniculus (Rabbit) |
| Cellular location | Endoplasmic reticulum membrane ; Multi-pass membrane protein : P04191 |
| Total number of polymer chains | 1 |
| Total formula weight | 136381.64 |
| Authors | Norimatsu, Y.,Hasegawa, K.,Shimizu, N.,Toyoshima, C. (deposition date: 2017-03-11, release date: 2017-05-24, Last modification date: 2024-10-16) |
| Primary citation | Norimatsu, Y.,Hasegawa, K.,Shimizu, N.,Toyoshima, C. Protein-phospholipid interplay revealed with crystals of a calcium pump. Nature, 545:193-198, 2017 Cited by PubMed Abstract: The lipid bilayer has so far eluded visualization by conventional crystallographic methods, severely limiting our understanding of phospholipid- and protein-phospholipid interactions. Here we describe electron density maps for crystals of Ca-ATPase in four different states obtained by X-ray solvent contrast modulation. These maps resolve the entire first layer of phospholipids surrounding the transmembrane helices, although less than half of them are hydrogen-bonded to protein residues. Phospholipids follow the movements of associated residues, causing local distortions and changes in thickness of the bilayer. Unexpectedly, the entire protein tilts during the reaction cycle, governed primarily by a belt of Trp residues, to minimize energy costs accompanying the large perpendicular movements of the transmembrane helices. A class of Arg residues extend their side chains through the cytoplasm to exploit phospholipids as anchors for conformational switching. Thus, phospholipid-Arg/Lys and phospholipid-Trp interactions have distinct functional roles in the dynamics of ion pumps and, presumably, membrane proteins in general. PubMed: 28467821DOI: 10.1038/nature22357 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.2 Å) |
Structure validation
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