Cloning, purification, crystallization and X-ray crystallographic analysis of the periplasmic sensing domain of Pseudomonas fluorescens chemotactic transducer of amino acids type A (CtaA)

Abu Iftiaf Md Salah Ud-Din, Anna Roujeinikova

Research output: Contribution to journalArticleResearchpeer-review

Abstract

Chemotaxis towards nutrients plays a crucial role in root colonization by Pseudomonas fluorescens. The P. fluorescens chemotactic transducer of amino acids type A (CtaA) mediates movement towards amino acids present in root exudates. In this study, the periplasmic sensory domain of CtaA has been crystallized by the hanging-drop vapor diffusion method using ammonium sulfate as a precipitating agent. A complete data set was collected to 1.9 Å resolution using cryocooling conditions and synchrotron radiation. The crystals belong to space group I222 or I212121, with unit-cell parameters a = 67.2, b = 76.0, c = 113.3 Å. This is an important step towards elucidation of the structural basis of how CtaA recognizes its signal molecules and transduces the signal across the membrane.
Original languageEnglish
Pages (from-to)320-324
Number of pages5
JournalBioScience Trends
Volume10
Issue number4
DOIs
Publication statusPublished - 2016

Keywords

  • Bacterial chemotaxis
  • Chemoreceptor
  • Sensing domain
  • Symbiosis

Cite this

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title = "Cloning, purification, crystallization and X-ray crystallographic analysis of the periplasmic sensing domain of Pseudomonas fluorescens chemotactic transducer of amino acids type A (CtaA)",
abstract = "Chemotaxis towards nutrients plays a crucial role in root colonization by Pseudomonas fluorescens. The P. fluorescens chemotactic transducer of amino acids type A (CtaA) mediates movement towards amino acids present in root exudates. In this study, the periplasmic sensory domain of CtaA has been crystallized by the hanging-drop vapor diffusion method using ammonium sulfate as a precipitating agent. A complete data set was collected to 1.9 {\AA} resolution using cryocooling conditions and synchrotron radiation. The crystals belong to space group I222 or I212121, with unit-cell parameters a = 67.2, b = 76.0, c = 113.3 {\AA}. This is an important step towards elucidation of the structural basis of how CtaA recognizes its signal molecules and transduces the signal across the membrane.",
keywords = "Bacterial chemotaxis, Chemoreceptor, Sensing domain, Symbiosis",
author = "Ud-Din, {Abu Iftiaf Md Salah} and Anna Roujeinikova",
year = "2016",
doi = "10.5582/bst.2016.01059",
language = "English",
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pages = "320--324",
journal = "BioScience Trends",
issn = "1881-7815",
publisher = "International Research and Cooperation Association for Bio & Socio-Sciences Advancement (IRCA-BSSA) Group",
number = "4",

}

Cloning, purification, crystallization and X-ray crystallographic analysis of the periplasmic sensing domain of Pseudomonas fluorescens chemotactic transducer of amino acids type A (CtaA). / Ud-Din, Abu Iftiaf Md Salah; Roujeinikova, Anna.

In: BioScience Trends, Vol. 10, No. 4, 2016, p. 320-324.

Research output: Contribution to journalArticleResearchpeer-review

TY - JOUR

T1 - Cloning, purification, crystallization and X-ray crystallographic analysis of the periplasmic sensing domain of Pseudomonas fluorescens chemotactic transducer of amino acids type A (CtaA)

AU - Ud-Din, Abu Iftiaf Md Salah

AU - Roujeinikova, Anna

PY - 2016

Y1 - 2016

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AB - Chemotaxis towards nutrients plays a crucial role in root colonization by Pseudomonas fluorescens. The P. fluorescens chemotactic transducer of amino acids type A (CtaA) mediates movement towards amino acids present in root exudates. In this study, the periplasmic sensory domain of CtaA has been crystallized by the hanging-drop vapor diffusion method using ammonium sulfate as a precipitating agent. A complete data set was collected to 1.9 Å resolution using cryocooling conditions and synchrotron radiation. The crystals belong to space group I222 or I212121, with unit-cell parameters a = 67.2, b = 76.0, c = 113.3 Å. This is an important step towards elucidation of the structural basis of how CtaA recognizes its signal molecules and transduces the signal across the membrane.

KW - Bacterial chemotaxis

KW - Chemoreceptor

KW - Sensing domain

KW - Symbiosis

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