3IXZ
Pig gastric H+/K+-ATPase complexed with aluminium fluoride
3IXZ の概要
エントリーDOI | 10.2210/pdb3ixz/pdb |
関連するPDBエントリー | 3B8E |
EMDBエントリー | 5104 |
分子名称 | Potassium-transporting ATPase alpha, Potassium-transporting ATPase subunit beta (2 entities in total) |
機能のキーワード | ion pump, h+, k+-atpase, p-type atpase, membrane protein, hydrolase, e2, aluminium fluoride, atp-binding, hydrogen ion transport, ion transport, magnesium, membrane, metal-binding, nucleotide-binding, phosphoprotein, potassium, potassium transport, transmembrane, transport, disulfide bond, glycoprotein, signal-anchor |
由来する生物種 | Sus scrofa (pigs,swine,wild boar) 詳細 |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 147513.53 |
構造登録者 | |
主引用文献 | Abe, K.,Tani, K.,Nishizawa, T.,Fujiyoshi, Y. Inter-subunit interaction of gastric H+,K+-ATPase prevents reverse reaction of the transport cycle Embo J., 28:1637-1643, 2009 Cited by PubMed Abstract: The gastric H(+),K(+)-ATPase is an ATP-driven proton pump responsible for generating a million-fold proton gradient across the gastric membrane. We present the structure of gastric H(+),K(+)-ATPase at 6.5 A resolution as determined by electron crystallography of two-dimensional crystals. The structure shows the catalytic alpha-subunit and the non-catalytic beta-subunit in a pseudo-E(2)P conformation. Different from Na(+),K(+)-ATPase, the N-terminal tail of the beta-subunit is in direct contact with the phosphorylation domain of the alpha-subunit. This interaction may hold the phosphorylation domain in place, thus stabilizing the enzyme conformation and preventing the reverse reaction of the transport cycle. Indeed, truncation of the beta-subunit N-terminus allowed the reverse reaction to occur. These results suggest that the beta-subunit N-terminus prevents the reverse reaction from E(2)P to E(1)P, which is likely to be relevant for the generation of a large H(+) gradient in vivo situation. PubMed: 19387495DOI: 10.1038/emboj.2009.102 主引用文献が同じPDBエントリー |
実験手法 | ELECTRON CRYSTALLOGRAPHY (6.5 Å) |
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