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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 : Structure (London, England : 1993)

Structural insights into the oligomerization and architecture of eukaryotic membrane pore-forming toxins

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Structure (London, England : 1993) - 09 Feb 2011

Mechaly AE, Bellomio A, Gil-Cartón D, Morante K, Valle M, González-Mañas JM, Guérin DM

Link to Pubmed [PMID] – 21300287

Structure 2011 Feb;19(2):181-91

Pore-forming toxins (PFTs) are proteins that are secreted as soluble molecules and are inserted into membranes to form oligomeric transmembrane pores. In this paper, we report the crystal structure of Fragaceatoxin C (FraC), a PFT isolated from the sea anemone Actinia fragacea, at 1.8 Å resolution. It consists of a crown-shaped nonamer with an external diameter of about 11.0 nm and an internal diameter of approximately 5.0 nm. Cryoelectron microscopy studies of FraC in lipid bilayers reveal the pore structure that traverses the membrane. The shape and dimensions of the crystallographic oligomer are fully consistent with the membrane pore. The FraC structure provides insight into the interactions governing the assembly process and suggests the structural changes that allow for membrane insertion. We propose a nonameric pore model that spans the membrane by forming a lipid-free α-helical bundle pore.

https://www.ncbi.nlm.nih.gov/pubmed/21300287