3J7T

Calcium atpase structure with two bound calcium ions determined by electron crystallography of thin 3D crystals

Summary for 3J7T

• Entry DOI: 10.2210/pdb3j7t/pdb
• Related: 1SU4 3J7U
• 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

Yonekura, K.,Kato, K.,Ogasawara, M.,Tomita, M.,Toyoshima, C. (deposition date: 2014-08-07, release date: 2015-02-18, Last modification date: 2024-11-13)

Primary citation

Yonekura, K.,Kato, K.,Ogasawara, M.,Tomita, M.,Toyoshima, C.
Electron crystallography of ultrathin 3D protein crystals: atomic model with charges
Proc.Natl.Acad.Sci.USA, 112:3368-3373, 2015

PubMed Abstract: Membrane proteins and macromolecular complexes often yield crystals too small or too thin for even the modern synchrotron X-ray beam. Electron crystallography could provide a powerful means for structure determination with such undersized crystals, as protein atoms diffract electrons four to five orders of magnitude more strongly than they do X-rays. Furthermore, as electron crystallography yields Coulomb potential maps rather than electron density maps, it could provide a unique method to visualize the charged states of amino acid residues and metals. Here we describe an attempt to develop a methodology for electron crystallography of ultrathin (only a few layers thick) 3D protein crystals and present the Coulomb potential maps at 3.4-Å and 3.2-Å resolution, respectively, obtained from Ca(2+)-ATPase and catalase crystals. These maps demonstrate that it is indeed possible to build atomic models from such crystals and even to determine the charged states of amino acid residues in the Ca(2+)-binding sites of Ca(2+)-ATPase and that of the iron atom in the heme in catalase.

PubMed: 25730881
DOI: 10.1073/pnas.1500724112

Experimental method

ELECTRON CRYSTALLOGRAPHY (3.4 Å)