Tanford C
Proc Natl Acad Sci U S A. 1982 May;79(9):2882-4. doi: 10.1073/pnas.79.9.2882.
The mechanism for active transport of ions across a membrane probably involves two distinct conformational states of the transport protein, in which the binding sites for the transported ion face opposite sides of the membrane. It is likely that the binding affinity for the ion changes in synchrony with the change in site orientation, such that the affinity is high on the uptake side of the membrane and low on the discharge side. A structural model is proposed for the transmembrane portion of such a protein, based on the known multihelical structure of bacteriorhodopsin. This structure is well adapted to a cyclical alternation between two conformations that differ simultaneously in orientation and binding affinity. No unfolding of the helices or other significant alterations in secondary structure is required. The model is explicitly intended as a hypothetical representation of the E1 and E2 states of ATP-driven Na+,K+ and Ca2+ pumps.
离子跨膜主动运输的机制可能涉及转运蛋白的两种不同构象状态,在这两种状态下,被转运离子的结合位点面向膜的两侧。离子的结合亲和力很可能与位点方向的变化同步改变,使得在膜的摄取侧亲和力高,而在释放侧亲和力低。基于已知的细菌视紫红质的多螺旋结构,提出了这种蛋白质跨膜部分的结构模型。这种结构非常适合于两种构象之间的周期性交替,这两种构象在方向和结合亲和力上同时不同。不需要螺旋展开或二级结构的其他重大改变。该模型明确旨在作为ATP驱动的Na +、K +和Ca2 +泵的E1和E2状态的假设表示。