| Literature DB >> 24915082 |
Shigeru Sugiyama1, Keiko Kashiwagi2, Keisuke Kakinouchi1, Hideyuki Tomitori2, Ken Kanai2, Michio Murata1, Hiroaki Adachi3, Hiroyoshi Matsumura3, Kazufumi Takano3, Satoshi Murakami3, Tsuyoshi Inoue3, Yusuke Mori3, Kazuei Igarashi4.
Abstract
A membrane-associated ATPase, PotA, is a component of the spermidine-preferential uptake system in prokaryotes that plays an important role in normal cell growth by regulating the cellular polyamine concentration. No three-dimensional structures of membrane-associated ATPases in polyamine-uptake systems have been determined to date. Here, the crystallization and preliminary X-ray diffraction analysis of PotA from Thermotoga maritima are reported. Diffraction data were collected and processed to 2.7 Å resolution from both native and selenomethionine-labelled crystals. Preliminary crystallographic analysis revealed that the crystals belonged to the hexagonal space group P3₁12 (or P3₂12), with unit-cell parameters a=b=88.9, c=221.2 Å, α=90, β=90, γ=120°, indicating that a dimer was present in the asymmetric unit.Entities:
Keywords: ABC transporter; PotA; Thermotoga maritima; polyamine-transport system
Mesh:
Substances:
Year: 2014 PMID: 24915082 PMCID: PMC4051526 DOI: 10.1107/S2053230X14008607
Source DB: PubMed Journal: Acta Crystallogr F Struct Biol Commun ISSN: 2053-230X Impact factor: 1.056