Abstract
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.
| Original language | English |
|---|---|
| Pages (from-to) | 741-748 |
| Number of pages | 8 |
| Journal | Journal of General Physiology |
| Volume | 122 |
| Issue number | 6 |
| DOIs | |
| State | Published - Dec 1 2003 |
| Externally published | Yes |
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Keywords
- Disulfide
- Helical screw
- S4 movement
- Shaker K channel
- Voltage gated
ASJC Scopus subject areas
- Physiology
Cite this
Molecular Movement of the Voltage Sensor in a K Channel. / Broomand, Amir; Männikkö, Roope; Larsson, Hans P; Elinder, Fredrik.
In: Journal of General Physiology, Vol. 122, No. 6, 01.12.2003, p. 741-748.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Molecular Movement of the Voltage Sensor in a K Channel
AU - Broomand, Amir
AU - Männikkö, Roope
AU - Larsson, Hans P
AU - Elinder, Fredrik
PY - 2003/12/1
Y1 - 2003/12/1
N2 - 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.
AB - 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.
KW - Disulfide
KW - Helical screw
KW - S4 movement
KW - Shaker K channel
KW - Voltage gated
UR - http://www.scopus.com/inward/record.url?scp=0345166933&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0345166933&partnerID=8YFLogxK
U2 - 10.1085/jgp.200308927
DO - 10.1085/jgp.200308927
M3 - Article
C2 - 14610021
AN - SCOPUS:0345166933
VL - 122
SP - 741
EP - 748
JO - Journal of General Physiology
JF - Journal of General Physiology
SN - 0022-1295
IS - 6
ER -