Three-dimensional structure of (Na+ + K+)-ATPase revealed by electron microscopy of two-dimensional crystals
| Autor: | A.V. Lunev, A.P. Kuzin, A.N. Barnakov, Yu.A. Ovchinnikov, Nikolai N. Modyanov, V.V. Demin, K.N. Dzhandzhugazyan |
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| Jazyk: | angličtina |
| Předmět: |
Models
Molecular Chemical Phenomena Protein Conformation Swine Two-dimensional crystal ATPase Biophysics Crystal structure Fluorescamine labelling Biochemistry law.invention Protein structure Image processing Structural Biology law Genetics Electron microscopy Animals Na+/K+-ATPase Molecular Biology Kidney Medulla biology Chemistry Resolution (electron density) Chemical modification Cell Biology Fluorescamine Microscopy Electron Crystallography Membrane biology.protein Sodium-Potassium-Exchanging ATPase Electron microscope Crystallization (Na+ +K+)-ATPase |
| Zdroj: | FEBS Letters. (1):73-76 |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/0014-5793(85)80430-0 |
| Popis: | Prolonged incubation of membrane fragments containing homogeneous (Na+ + K+)-ATPase with Mg2+, K+ and VO-3 at 4 degrees C resulted in formation of two-dimensional crystals of this enzyme with unit cell parameters: a = 66 A, b = 118 A, gamma = 108 degrees. The crystals correspond to the two-sided plane group p21. By combining tilted electron microscopic views of the crystals, a three-dimensional structure of (Na+ + K+)- ATPase was calculated at approximately 20 A resolution. The unit cell is formed by two (alpha beta)-promoters which are in contact in their central parts. The structure was compared with chemical modification and immunochemical data; the arrangement of intra- and extramembrane domains was proposed. |
| Databáze: | OpenAIRE |
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