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The crystal structure of GXGD membrane protease FlaK

Author

Listed:
  • Jian Hu

    (Yale School of Medicine)

  • Yi Xue

    (Yale School of Medicine)

  • Sangwon Lee

    (Yale School of Medicine)

  • Ya Ha

    (Yale School of Medicine)

Abstract

Membrane aspartyl protease structure The GXGD family of intramembrane proteases includes presenilin, which is mutated in familial Alzheimer's disease, and type 4 prepilin peptidases, which are virulence factors for many pathogenic bacteria. The first crystal structure of a GXGD membrane protease has now been determined. The structure of the FlaK preflagellin peptidase from Methanococcus maripaludis reveals fundamental differences between the GXGD membrane aspartyl protease and its soluble counterparts such as pepsin. Comparison with models of presenilin derived from biochemical analysis suggests that the structure of its active site is similar to that of archaeal FlaK. This structural knowledge will facilitate rational design of inhibitors that target this family of proteases.

Suggested Citation

  • Jian Hu & Yi Xue & Sangwon Lee & Ya Ha, 2011. "The crystal structure of GXGD membrane protease FlaK," Nature, Nature, vol. 475(7357), pages 528-531, July.
    • Handle: RePEc:nat:nature:v:475:y:2011:i:7357:d:10.1038_nature10218
    DOI: 10.1038/nature10218
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    Cited by:

    1. Yao Zhang & Yuhan Jiang & Kaifu Gao & Dexin Sui & Peixuan Yu & Min Su & Guo-Wei Wei & Jian Hu, 2023. "Structural insights into the elevator-type transport mechanism of a bacterial ZIP metal transporter," Nature Communications, Nature, vol. 14(1), pages 1-14, December.

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