Two-dimensional crystals of membrane-bound gastric H,K-ATPase.
Two-dimensional crystallization of membrane-bound H,K-ATPase (EC 3.6.1.36) in vesicle preparations from parietal cells of hog gastric mucosa was induced by an imidazole buffer containing Mg2+ and VO3- ions. A continuous reorganization of the protein molecules started within a few hours by the formation of linear arrays. At later stages confluent two-dimensional crystals were formed. Electron microscopy and image processing showed that these were of a single tetragonal type. The asymmetric unit consisted of one pear-shaped protein domain corresponding to a H,K-ATPase protomer. Through stain-deficient contact regions four adjacent protein units were connected forming a tetrameric structure.
Hebert
H
H
Center for Structural Biochemistry, Karolinska Institute, Novum, Huddinge, Sweden.
Xian
Y
Y
Hacksell
I
I
Mårdh
S
S
D000251:Adenosine Triphosphatases / Q000378:metabolism* / Q000648:ultrastructure; D000818:Animals; D003460:Crystallization; D005753:Gastric Mucosa / Q000201:enzymology*; D017506:H(+)-K(+)-Exchanging ATPase; D008565:Membrane Proteins / Q000378:metabolism*; D008854:Microscopy, Electron; D013552:Swine; D014961:X-Ray Diffraction
D008565:Membrane Proteins; D000251:Adenosine Triphosphatases; D017506:H(+)-K(+)-Exchanging ATPase