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326 a.a.
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386 a.a.
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363 a.a.
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* Residue conservation analysis
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PDB id:
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Membrane protein, transport protein
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Title:
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Shaker family voltage dependent potassium channel (kv1.2-kv2.1 paddle chimera channel) in association with beta subunit
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Structure:
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Voltage-gated potassium channel subunit beta-2. Chain: a, g. Synonym: k+, channel subunit beta-2, kv-beta-2. Engineered: yes. Paddle chimera voltage gated potassium channel kv1.2-kv2.1. Chain: b, h. Engineered: yes
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Source:
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Rattus norvegicus. Norway rat. Organism_taxid: 10116. Gene: kcnab2, ckbeta2, kcnb3. Expressed in: pichia pastoris. Expression_system_taxid: 4922. Gene: kcna2. Expression_system_taxid: 4922
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Resolution:
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2.40Å
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R-factor:
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0.212
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R-free:
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0.244
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Authors:
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S.B.Long,X.Tao,E.B.Campbell,R.Mackinnon
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Key ref:
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S.B.Long
et al.
(2007).
Atomic structure of a voltage-dependent K+ channel in a lipid membrane-like environment.
Nature,
450,
376-382.
PubMed id:
DOI:
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Date:
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13-Sep-07
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Release date:
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20-Nov-07
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PROCHECK
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Headers
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References
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P62483
(KCAB2_RAT) -
Voltage-gated potassium channel subunit beta-2 from Rattus norvegicus
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Seq:
Struc:
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367 a.a.
326 a.a.
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DOI no:
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Nature
450:376-382
(2007)
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PubMed id:
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Atomic structure of a voltage-dependent K+ channel in a lipid membrane-like environment.
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S.B.Long,
X.Tao,
E.B.Campbell,
R.MacKinnon.
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ABSTRACT
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Voltage-dependent K+ (Kv) channels repolarize the action potential in neurons
and muscle. This type of channel is gated directly by membrane voltage through
protein domains known as voltage sensors, which are molecular voltmeters that
read the membrane voltage and regulate the pore. Here we describe the structure
of a chimaeric voltage-dependent K+ channel, which we call the 'paddle-chimaera
channel', in which the voltage-sensor paddle has been transferred from Kv2.1 to
Kv1.2. Crystallized in complex with lipids, the complete structure at 2.4
ångström resolution reveals the pore and voltage sensors embedded in a
membrane-like arrangement of lipid molecules. The detailed structure, which can
be compared directly to a large body of functional data, explains charge
stabilization within the membrane and suggests a mechanism for voltage-sensor
movements and pore gating.
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Selected figure(s)
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Figure 4.
Figure 4: Details of the voltage sensor. a, Stereo
representation of a voltage sensor and the S4–S5 linker helix
(white  -carbon
trace) in relation to the pore (cyan -carbon
trace). The view is from the side (extracellular solution
'above' and intracellular solution 'below'). Select residues are
shown as sticks and are coloured as indicated in the text. b,
Voltage sensor and S4–S5 linker helix (white -carbon
trace) viewed from the pore. Yellow side chains from a and water
molecules are now coloured according to atom type (yellow,
carbon; blue, nitrogen; red, oxygen; green, phenylalanine 233;
cyan, water). Ionized hydrogen bonds between basic and acidic
residues are indicated by dashed yellow lines.
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Figure 6.
Figure 6: Hypothetical mechanism of voltage-dependent gating.
a, Representation of the voltage sensor and S4–S5 linker helix
from the crystal structure (open conformation). Helices are
drawn as ribbons. The view is from the pore, as in Fig. 5, with
the extracellular solution 'above' and the intracellular
solution 'below'. The gating charges (R1 to K5) are shown as
blue sticks. Negatively charged residues in the external and
internal clusters are red; the phenylalanine in the middle is
green. The positively charged residues reach 'outward' towards
the extracellular solution. b, Depiction of a hypothetical
closed conformation of the voltage sensor. The S1 and S2 helices
are hypothesized to maintain their position, whereas the S3–S4
paddle has moved inward. The positive charges on S4 now reach
towards the intracellular solution, and are stabilized through
interactions with the internal negative cluster. The -carbon
position of R1 is adjacent to the phenylalanine, representing a
displacement perpendicular to the plane of the membrane of
approximately 15 Å relative to its location in the open
structure (a). The inward displacement of the S4 helix pushes
down on the N-terminal end of the S4–S5 linker helix, causing
it to tilt towards the intracellular side and to close the pore.
c, Depiction of the open conformation of the S4–S5 linker
helices and pore from the crystal structure. The S4–S5 linker
helices (orange) rest on the S6 helices (blue ribbons) near the
intracellular side. d, A hypothetical model of the S4–S5
linker helices and pore in a closed conformation based on the
crystal structure of a closed potassium channel pore (KcsA, PDB
accession number, 1K4C)^18.
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The above figures are
reprinted
by permission from Macmillan Publishers Ltd:
Nature
(2007,
450,
376-382)
copyright 2007.
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Figures were
selected
by an automated process.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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J.Payandeh,
T.M.Gamal El-Din,
T.Scheuer,
N.Zheng,
and
W.A.Catterall
(2012).
Crystal structure of a voltage-gated sodium channel in two potentially inactivated states.
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Nature,
486,
135-139.
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PDB code:
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X.Zhang,
W.Ren,
P.DeCaen,
C.Yan,
X.Tao,
L.Tang,
J.Wang,
K.Hasegawa,
T.Kumasaka,
J.He,
J.Wang,
D.E.Clapham,
and
N.Yan
(2012).
Crystal structure of an orthologue of the NaChBac voltage-gated sodium channel.
|
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Nature,
486,
130-134.
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PDB code:
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|
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A.Choutko,
A.Glättli,
C.Fernández,
C.Hilty,
K.Wüthrich,
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C.Gajewski,
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and
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(2011).
Biogenesis of the pore architecture of a voltage-gated potassium channel.
|
| |
Proc Natl Acad Sci U S A,
108,
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Mapping the sequence of conformational changes underlying selectivity filter gating in the K(v)11.1 potassium channel.
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|
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J.Payandeh,
T.Scheuer,
N.Zheng,
and
W.A.Catterall
(2011).
The crystal structure of a voltage-gated sodium channel.
|
| |
Nature,
475,
353-358.
|
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|
PDB codes:
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K.Illergård,
A.Kauko,
and
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and
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R.Verma,
and
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|
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|
| |
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PDB codes:
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|
|
V.Jimenez,
M.Henriquez,
N.Galanti,
and
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(2011).
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and
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| |
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|
| |
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| |
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|
|
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|
|
|
|
A.Yeheskel,
T.Haliloglu,
and
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(2010).
Independent and cooperative motions of the Kv1.2 channel: voltage sensing and gating.
|
| |
Biophys J,
98,
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|
|
|
|
|
|
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B.Musset,
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D.Morgan,
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|
| |
J Physiol,
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|
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|
|
|
C.Gonzalez,
H.P.Koch,
B.M.Drum,
and
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(2010).
Strong cooperativity between subunits in voltage-gated proton channels.
|
| |
Nat Struct Mol Biol,
17,
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|
|
|
|
|
|
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C.Gonzalez,
and
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(2010).
Permeation mechanism in voltage-activated proton channels: a new glimpse.
|
| |
Proc Natl Acad Sci U S A,
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|
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and
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Interactions between a voltage sensor and a toxin via multiscale simulations.
|
| |
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|
|
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D.G.Gagnon,
and
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The contribution of individual subunits to the coupling of the voltage sensor to pore opening in Shaker K channels: effect of ILT mutations in heterotetramers.
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| |
J Gen Physiol,
136,
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NMR analysis of the alphaIIb beta3 cytoplasmic interaction suggests a mechanism for integrin regulation.
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| |
Proc Natl Acad Sci U S A,
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PDB code:
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D.Pogoryelov,
A.Krah,
J.D.Langer,
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| |
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PDB code:
|
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|
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Z.Ma,
K.Y.Wong,
and
F.T.Horrigan
(2008).
An extracellular Cu2+ binding site in the voltage sensor of BK and Shaker potassium channels.
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| |
J Gen Physiol,
131,
483-502.
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M.C.Lin,
and
D.M.Papazian
(2007).
Differences between ion binding to eag and HERG voltage sensors contribute to differential regulation of activation and deactivation gating.
|
| |
Channels (Austin),
1,
429-437.
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|
|
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|
The most recent references are shown first.
Citation data come partly from CiteXplore and partly
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only a partial list as not all journals are covered by
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so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
code is
shown on the right.
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