3vou | pdb_00003vou

The crystal structure of NaK-NavSulP chimera channel

Loading... Status: waiting for Mol* initialization Structural highlights 3vou is a 2 chain structure with sequence from Bacillus mycoides KBAB4 and Sulfitobacter sp. NAS-14.1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.2Å Ligands: CO, NA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A3SUL8_SULSN A9VEV6_BACMK Publication Abstract from PubMed Most tetrameric channels have cytosolic domains to regulate their functions, including channel inactivation. Here we show that the cytosolic C-terminal region of NavSulP, a prokaryotic voltage-gated sodium channel cloned from Sulfitobacter pontiacus, accelerates channel inactivation. The crystal structure of the C-terminal region of NavSulP grafted into the C-terminus of a NaK channel revealed that the NavSulP C-terminal region forms a four-helix bundle. Point mutations of the residues involved in the intersubunit interactions of the four-helix bundle destabilized the tetramer of the channel and reduced the inactivation rate. The four-helix bundle was directly connected to the inner helix of the pore domain, and a mutation increasing the rigidity of the inner helix also reduced the inactivation rate. These findings suggest that the NavSulP four-helix bundle has important roles not only in stabilizing the tetramer, but also in accelerating the inactivation rate, through promotion of the conformational change of the inner helix. The C-terminal helical bundle of the tetrameric prokaryotic sodium channel accelerates the inactivation rate.,Irie K, Shimomura T, Fujiyoshi Y Nat Commun. 2012 Apr 24;3:793. doi: 10.1038/ncomms1797. PMID:22531178 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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