Aharoni A, Horovitz A
Department of Structural Biology, Weizmann Institute of Science, Rehovot, Israel.
J Mol Biol. 1996 May 24;258(5):732-5. doi: 10.1006/jmbi.1996.0282.
The crystal structures of the chaperonin GroEL Arg13 --> Gly; Ala126 --> Val double mutant, without and in complex with ATP gamma S, have been determined at atomic resolution. Here, we show that the double mutation Arg13 --> Gly; Ala126 --> Val disrupts negative co-operativity between GroEL rings, with respect to ATP, but has little effect on the positive co-operativity within each ring. Our results help to explain why the double mutation facilitated the crystallization of GroEL and why breaking of dyad symmetry between rings is not observed in crystal structures of this mutant. Our results may also help to explain why the observed structural differences between the GroEL double mutant and its ATP gamma S-bound form are small.
伴侣蛋白GroEL的精氨酸13突变为甘氨酸;丙氨酸126突变为缬氨酸的双突变体,在没有ATPγS以及与ATPγS结合的情况下的晶体结构已在原子分辨率下确定。在此,我们表明,精氨酸13突变为甘氨酸;丙氨酸126突变为缬氨酸的双突变破坏了GroEL环之间关于ATP的负协同性,但对每个环内的正协同性影响很小。我们的结果有助于解释为什么双突变促进了GroEL的结晶,以及为什么在该突变体的晶体结构中未观察到环之间二重对称轴的破坏。我们的结果也可能有助于解释为什么观察到的GroEL双突变体与其ATPγS结合形式之间的结构差异很小。