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Figure 1

Figure 1. Conformation states of a membrane transporter. From: Biophysics: Transporter in the spotlight.

The LeuT protein adopts various conformational states as it transports the amino acid leucine across bacterial cell membranes. It consists of a pore containing two gates, the inner and outer gates. Four conformational states are shown here; the total number of states is unknown. a, The transport cycle begins with an outward-facing state, Co, in which the outer gate is open but the inner gate is closed. b, The binding of a leucine molecule and a sodium ion at sites between the gates causes the outer gate to close, generating the occluded state (Occ). c, A second leucine molecule can then bind to another site just outside the outer gate. d, Next, LeuT opens its inner gate and loses all its substrates to form the inward-facing state, Ci. Closure of the inner and gate and opening of the outer gate returns LeuT to the Co state. Zhao et al.4 have used a fluorescence-based, single-molecule technique to study the transition between Ci and Co.

Nathan K. Karpowich, et al. Nature. ;465(7295):171-172.

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