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Crystallization and preliminary crystallographic studies of PotA, a membrane‐associated ATPase of the spermidine‐preferential uptake system in Thermotoga maritima
Author(s) -
Sugiyama Shigeru,
Kashiwagi Keiko,
Kakinouchi Keisuke,
Tomitori Hideyuki,
Kanai Ken,
Murata Michio,
Adachi Hiroaki,
Matsumura Hiroyoshi,
Takano Kazufumi,
Murakami Satoshi,
Inoue Tsuyoshi,
Mori Yusuke,
Igarashi Kazuei
Publication year - 2014
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x14008607
Subject(s) - thermotoga maritima , crystallization , crystallography , polyamine , dimer , atpase , chemistry , membrane , spermidine , biophysics , biochemistry , biology , enzyme , gene , escherichia coli , organic chemistry
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 P 3 1 12 (or P 3 2 12), 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.