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© Ahmed Haouz
Cristaux d'une protéine de Mycobacterium tuberculosis produits dans le cadre du Grand Programme Horizontal sur la Tuberculose à l'Institut Pasteur. La caractérisation structurale de protéines mycobactériennes aide à une meilleure compréhension de la physiologie et de la pathogénicité des mycobactéries et fournit un point de départ pour la conception de nouveaux agents antibactériens.
Publication : Acta crystallographica. Section F, Structural biology and crystallization communications

Crystallization and preliminary crystallographic analysis of fragaceatoxin C, a pore-forming toxin from the sea anemone Actinia fragacea

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Acta crystallographica. Section F, Structural biology and crystallization communications - 21 Mar 2009

Mechaly AE, Bellomio A, Morante K, González-Mañas JM, Guérin DM

Link to Pubmed [PMID] – 19342779

Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 2009 Apr;65(Pt 4):357-60

Sea anemones produce water-soluble toxins that have the ability to interact with cell membranes and form pores within them. The mechanism of pore formation is based on an initial binding step followed by oligomerization and membrane insertion. Although the final structure of the pore remains unclear, biochemical studies indicate that it consists of a tetramer with a functional radius of approximately 1.1 nm. Since four monomers seem to be insufficient to build a pore of this size, the currently accepted model suggests that lipids might also participate in its structure. In this work, the crystallization and preliminary crystallographic analysis of two crystal forms of fragaceatoxin C (FraC), a newly characterized actinoporin from Actinia fragacea, are described. The crystals diffracted up to 1.8 A resolution and the preliminary molecular-replacement solution supports an oligomeric structure of about 120 A in diameter.

https://www.ncbi.nlm.nih.gov/pubmed/19342779