Crystallization and preliminary crystallographic studies of PotA, a membrane‐associated ATPase of the spermidine‐preferential uptake system in Thermotoga maritima. Issue 6 (1st June 2014)

• Record Type: Journal Article
• Authors: 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
• Is Part Of: Acta crystallographica. Volume 70:Issue 6(2014:Jun.)
• Page Start: 738
• Page End: 741
• Publication Date: 2014-06-01
• Subjects: Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S2053230X14008607
• Languages: English
• ISSNs: 2053-230X

Abstract

<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p>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 <italic>Thermotoga maritima</italic> 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 <italic>P</italic>3₁12 (or <italic>P</italic>3₂12), with unit‐cell parameters <italic>a</italic> = <italic>b</italic> = 88.9, <italic>c</italic> = 221.2 Å, α = 90, β = 90, γ = 120°, indicating that a dimer was present in the asymmetric unit.</p> </abstract>