Figure 3 (IMAGE)
Caption
Allosteric communications between two rings of GroEL. The lifetime distribution of bound GroES was best fitted to a sequential four step reaction model with four rate constants, k1, k2, k3 and k4. The value of k3 agreed with that of the rate of bullet-to-football transition (kBF) in the opposite ring. Moreover, the value of 1/k1 + 1/k2 agreed with that of 1/kFB (kFB, the rate of football-to-bullet transition in the opposite ring). The former agreement indicates that ATP hydrolysis into ADP-Pi on one ring acts as a time keeper for ADP release from the opposite trans ring, ensuring the release of substrate protein from the trans-ring before it is capped with GroES. The latter agreement indicates that an event occurring in the second step after ATP binding triggers Pi release from the opposite ring.
Credit
Kanazawa University
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