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Molecular Movement of the Voltage Sensor in a K Channel
2 Neurological Sciences Institute, Oregon Health and Science University, Beaverton, OR 97006
Address correspondence to Fredrik Elinder, Department of Neuroscience, Retzius väg 8, Karolinska Institutet, SE-171 77 Stockholm, Sweden. Fax: (46) 8-34 95 44; email: fredrik.elinder{at}neuro.ki.se
The X-ray crystallographic structure of KvAP, a voltage-gated bacterial K channel, was recently published. However, the position and the molecular movement of the voltage sensor, S4, are still controversial. For example, in the crystallographic structure, S4 is located far away (>30 Å) from the pore domain, whereas electrostatic experiments have suggested that S4 is located close (<8 Å) to the pore domain in open channels. To test the proposed location and motion of S4 relative to the pore domain, we induced disulphide bonds between pairs of introduced cysteines: one in S4 and one in the pore domain. Several residues in S4 formed a state-dependent disulphide bond with a residue in the pore domain. Our data suggest that S4 is located close to the pore domain in a neighboring subunit. Our data also place constraints on possible models for S4 movement and are not compatible with a recently proposed KvAP model.
Key Words: Shaker K channel • voltage gated • disulfide • S4 movement • helical screw
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