Ligand binding and conformational states of the photoprotein obelin

Описание

Тип публикации: статья из журнала

Год издания: 2012

Идентификатор DOI: 10.1016/j.febslet.2012.10.015

Ключевые слова: Bioluminescence, Coelenterazine, Photoprotein, Thermostability, Bioluminescence, Coelenterazine, Photoprotein, Thermostability, calcium, photoprotein, photoprotein obelin, unclassified drug, article, circular dichroism, ligand binding, priority journal, protein conformation, protein expression, protein function, protein purification, protein stability, protein structure, protein unfolding, structure analysis, Calcium, Circular Dichroism, Imidazoles, Luminescent Proteins, Protein Binding, Protein Folding, Pyrazines, Spectrometry, Fluorescence

Аннотация: Many proteins require a non-covalently bound ligand to be functional. How ligand binding affects protein conformation is often unknown. Here we address thermal unfolding of the free and ligand-bound forms of photoprotein obelin. Fluorescence and far-UV circular dichroism ( CD) data show that the various ligand-dependent conformatioПоказать полностьюnal states of obelin differ significantly in stability against thermal unfolding. Binding of coelenterazine and calcium considerably stabilizes obelin. In solution, all obelin structures are similar, except for apo-obelin without calcium. This latter protein is an ensemble of conformational states, the populations of which alter upon increasing temperature. (C) 2012 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.

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Издание

Журнал: FEBS LETTERS

Выпуск журнала: Vol. 586, Is. 23

Номера страниц: 4173-4179

ISSN журнала: 00145793

Место издания: AMSTERDAM

Издатель: ELSEVIER SCIENCE BV

Авторы

  • Eremeeva Elena V. (Wageningen Univ, Biochem Lab, NL-6703 HA Wageningen, Netherlands; Russian Acad Sci, Photobiol Lab, Inst Biophys, Siberian Branch, Krasnoyarsk 660036, Russia; Siberian Fed Univ, Lab Bioluminescence Biotechnol, Inst Fundamental Biol & Biotechnol, Krasnoyarsk 660041, Russia)
  • Vysotski Eugene S. (Russian Acad Sci, Photobiol Lab, Inst Biophys, Siberian Branch, Krasnoyarsk 660036, Russia; Siberian Fed Univ, Lab Bioluminescence Biotechnol, Inst Fundamental Biol & Biotechnol, Krasnoyarsk 660041, Russia)
  • Westphal Adrie H. (Wageningen Univ, Biochem Lab, NL-6703 HA Wageningen, Netherlands)
  • van Mierlo Carlo P. M. (Wageningen Univ, Biochem Lab, NL-6703 HA Wageningen, Netherlands)
  • van Berkel Willem J. H. (Wageningen Univ, Biochem Lab, NL-6703 HA Wageningen, Netherlands)

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