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Journal Articles Nature Structural Biology Year : 2002

The crystal structure of the mouse apoptosis-inducing factor AIF

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Ahmed Haouz
Santos A. Susin
Guido Kroemer
Pedro Alzari
  • Function : Correspondent author
  • PersonId : 923367

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Abstract

Mitochondria play a key role in apoptosis due to their capacity to release potentially lethal proteins. One of these latent death factors is cytochrome c, which can stimulate the proteolytic activation of caspase zymogens. Another important protein is apoptosis-inducing factor (AIF), a flavoprotein that can stimulate a caspase-independent cell-death pathway required for early embryonic morphogenesis. Here, we report the crystal structure of mouse AIF at 2.0 A. Its active site structure and redox properties suggest that AIF functions as an electron transferase with a mechanism similar to that of the bacterial ferredoxin reductases, its closest evolutionary homologs. However, AIF structurally differs from these proteins in some essential features, including a long insertion in a C-terminal beta-hairpin loop, which may be related to its apoptogenic functions.
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Dates and versions

pasteur-03144692 , version 1 (17-02-2021)

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María J. Maté, Miguel Ortiz-Lombardía, Brigitte Boitel, Ahmed Haouz, Diana Tello, et al.. The crystal structure of the mouse apoptosis-inducing factor AIF. Nature Structural Biology, 2002, 9 (6), pp.442-6. ⟨10.1038/nsb793⟩. ⟨pasteur-03144692⟩
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