Literature DB >> 24915082

Crystallization and preliminary crystallographic studies of PotA, a membrane-associated ATPase of the spermidine-preferential uptake system in Thermotoga maritima.

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


  20 in total

1.  Identification of the putrescine recognition site on polyamine transport protein PotE.

Authors:  K Kashiwagi; A Kuraishi; H Tomitori; A Igarashi; K Nishimura; A Shirahata; K Igarashi
Journal:  J Biol Chem       Date:  2000-11-17       Impact factor: 5.157

2.  Crystallization and preliminary X-ray analysis of the primary receptor (PotD) of the polyamine transport system in Escherichia coli.

Authors:  S Sugiyama; M Matsushima; T Saisho; K Kashiwagi; K Igarashi; K Morikawa
Journal:  Acta Crystallogr D Biol Crystallogr       Date:  1996-03-01

3.  Excretion and uptake of putrescine by the PotE protein in Escherichia coli.

Authors:  K Kashiwagi; S Shibuya; H Tomitori; A Kuraishi; K Igarashi
Journal:  J Biol Chem       Date:  1997-03-07       Impact factor: 5.157

4.  Excretion of putrescine by the putrescine-ornithine antiporter encoded by the potE gene of Escherichia coli.

Authors:  K Kashiwagi; S Miyamoto; F Suzuki; H Kobayashi; K Igarashi
Journal:  Proc Natl Acad Sci U S A       Date:  1992-05-15       Impact factor: 11.205

5.  Solvent content of protein crystals.

Authors:  B W Matthews
Journal:  J Mol Biol       Date:  1968-04-28       Impact factor: 5.469

6.  Crystal structure of PotD, the primary receptor of the polyamine transport system in Escherichia coli.

Authors:  S Sugiyama; D G Vassylyev; M Matsushima; K Kashiwagi; K Igarashi; K Morikawa
Journal:  J Biol Chem       Date:  1996-04-19       Impact factor: 5.157

Review 7.  Polyamine transport in bacteria and yeast.

Authors:  K Igarashi; K Kashiwagi
Journal:  Biochem J       Date:  1999-12-15       Impact factor: 3.857

Review 8.  Modulation of cellular function by polyamines.

Authors:  Kazuei Igarashi; Keiko Kashiwagi
Journal:  Int J Biochem Cell Biol       Date:  2009-07-28       Impact factor: 5.085

9.  Isolation and characterization of a cDNA clone that codes for human spermidine/spermine N1-acetyltransferase.

Authors:  R A Casero; P Celano; S J Ervin; N B Applegren; L Wiest; A E Pegg
Journal:  J Biol Chem       Date:  1991-01-15       Impact factor: 5.157

Review 10.  Polyamine metabolism and its importance in neoplastic growth and a target for chemotherapy.

Authors:  A E Pegg
Journal:  Cancer Res       Date:  1988-02-15       Impact factor: 12.701

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