PDBsum entry 3a2a

Transport protein

PDB id: 3a2a

Contents

Protein chain

41 a.a.

Metals

_CL ×2

Waters ×68

PDB id:

3a2a

Name:

Transport protein

Title:

The structure of the carboxyl-terminal domain of the human voltage- gated proton channel hv1

Structure:

Voltage-gated hydrogen channel 1. Chain: a, b, c, d. Fragment: c-terminal domain, unp residues 221-273. Synonym: hydrogen voltage-gated channel 1, hv1, voltage sensor domain-only protein. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.00Å R-factor: 0.253 R-free: 0.266

Authors:

S.J.Li,H.Unno,Q.Zhou,Q.Zhao,Y.Zhai,F.Sun

Key ref:

S.J.Li et al. (2010). The role and structure of the carboxyl-terminal domain of the human voltage-gated proton channel Hv1. J Biol Chem, 285, 12047-12054. PubMed id: 20147290

Date:

08-May-09 Release date: 09-Feb-10

Protein chains

Q96D96  (HVCN1_HUMAN) -  Voltage-gated hydrogen channel 1 from Homo sapiens

Seq: 273 a.a.

Struc: 41 a.a.

J Biol Chem 285:12047-12054 (2010)

PubMed id: 20147290

The role and structure of the carboxyl-terminal domain of the human voltage-gated proton channel Hv1.

S.J.Li, Q.Zhao, Q.Zhou, H.Unno, Y.Zhai, F.Sun.

ABSTRACT

The voltage-gated proton channel Hv1 has a voltage sensor domain but lacks a pore domain. Although the C-terminal domain of Hv1 is known to be responsible for dimeric architecture of the channel, its role and structure are not known. We report that the full-length Hv1 is mainly localized in intracellular compartment membranes rather than the plasma membrane. Truncation of either the N or C terminus alone or both together revealed that the N-terminal deletion did not alter localization, but deletion of the C terminus either alone or together with the N terminus resulted in expression throughout the cell. These results indicate that the C terminus is essential for Hv1 localization but not the N terminus. In the 2.0 A structure of the C-terminal domain, the two monomers form a dimer via a parallel alpha-helical coiled-coil, in which one chloride ion binds with the Neta atom of Arg(264). A pH-dependent structural change of the protein has been observed, but it remains a dimer irrespective of pH value.