PDBsum entry 2a0l

Membrane protein

PDB id: 2a0l

Contents

Protein chains

214 a.a. *

105 a.a. *

116 a.a. *

Metals

__K ×4

* Residue conservation analysis

PDB id:

2a0l

Name:

Membrane protein

Title:

Crystal structure of kvap-33h1 fv complex

Structure:

Voltage-gated potassium channel. Chain: a, b. Fragment: kvap k+ channel. Synonym: kvap. Engineered: yes. 33h1 fv fragment. Chain: c, e. Fragment: fv fragment,light chain. 33h1 fv fragment.

Source:

Aeropyrum pernix. Organism_taxid: 56636. Gene: kvap_aerpe. Expressed in: escherichia coli. Expression_system_taxid: 562. Mus musculus. House mouse. Organism_taxid: 10090. Other_details: mouse hybridoma.

Resolution:

3.90Å R-factor: 0.358 R-free: 0.392

Authors:

S.Y.Lee,A.Lee,J.Chen,R.Mackinnon

Key ref:

S.Y.Lee et al. (2005). Structure of the KvAP voltage-dependent K+ channel and its dependence on the lipid membrane. Proc Natl Acad Sci U S A, 102, 15441-15446. PubMed id: 16223877 DOI: 10.1073/pnas.0507651102

Date:

16-Jun-05 Release date: 01-Nov-05

Protein chains

Q9YDF8  (KVAP_AERPE) -  Voltage-gated potassium channel from Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)

Seq: 295 a.a.

Struc: 214 a.a.

Protein chains

No UniProt id for this chain

Struc: 105 a.a.

Protein chains

No UniProt id for this chain

Struc: 116 a.a.

DOI no: 10.1073/pnas.0507651102

Proc Natl Acad Sci U S A 102:15441-15446 (2005)

PubMed id: 16223877

Structure of the KvAP voltage-dependent K+ channel and its dependence on the lipid membrane.

S.Y.Lee, A.Lee, J.Chen, R.MacKinnon.

ABSTRACT

Voltage-dependent ion channels gate open in response to changes in cell membrane voltage. This form of gating permits the propagation of action potentials. We present two structures of the voltage-dependent K(+) channel KvAP, in complex with monoclonal Fv fragments (3.9 A) and without antibody fragments (8 A). We also studied KvAP with disulfide cross-bridges in lipid membranes. Analyzing these data in the context of the crystal structure of Kv1.2 and EPR data on KvAP we reach the following conclusions: (i) KvAP is similar in structure to Kv1.2 with a very modest difference in the orientation of its voltage sensor; (ii) mAb fragments are not the source of non-native conformations of KvAP in crystal structures; (iii) because KvAP contains separate loosely adherent domains, a lipid membrane is required to maintain their correct relative orientations, and (iv) the model of KvAP is consistent with the proposal of voltage sensing through the movement of an arginine-containing helix-turn-helix element at the protein-lipid interface.

Selected figure(s)

Figure 2.
Fig. 2. Structure of the KvAP-33HI complex and comparison with previous KvAP structures. (a) Stereo view of a single KvAP subunit from the side with extracellular solution above. S1-S4 helices are colored blue. (b) Stereo view of a single KvAP subunit of the KvAP-6E1 Fab complex (PDB ID code 1ORQ [PDB] ). (c) Comparison with the isolated voltage sensor structure. Stereo view of a superposition of the isolated voltage sensor (gold, PDB ID code 1ORS [PDB] ) and the KvAP-Fv complex (blue). The S2 helix (Leu-55 to Tyr-75) was used for superposition, and the S1 helix is not shown. Residues Asp-62, Asp-72, Arg-76, Glu-93, and Arg-133, which are important for channel function, are shown in ball-and-stick representation.

Figure 6.
Fig. 6. A model of the KvAP tetramer in the open conformation. The top-down view (a) and the side view (b) of the proposed model of the KvAP tetramer in the open conformation. Each subunit is colored blue, green, gold, and red. This model is the same as in Fig. 4b but it is shown as a tetramer to show the position of the voltage sensor relative to the pore.

Figures were selected by an automated process.