Large lateral movement of transmembrane helix S5 is not required for substrate access to the active site of rhomboid intramembrane protease.

@article{Xue2013LargeLM,
  title={Large lateral movement of transmembrane helix S5 is not required for substrate access to the active site of rhomboid intramembrane protease.},
  author={Yi Long Xue and Ya Ha},
  journal={The Journal of biological chemistry},
  year={2013},
  volume={288 23},
  pages={16645-54}
}
Rhomboids represent an evolutionarily ancient protease family. Unlike most other proteases, they are polytopic membrane proteins and specialize in cleaving transmembrane protein substrates. The polar active site of rhomboid protease is embedded in the membrane and normally closed. For the bacterial rhomboid GlpG, it has been proposed that one of the transmembrane helices (S5) of the protease can rotate to open a lateral gate, enabling substrate to enter the protease from inside the membrane… CONTINUE READING

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Enzymatic analysis of a rhomboid intramembrane protease implicates transmembrane helix 5 as the lateral substrate gate.

Proceedings of the National Academy of Sciences of the United States of America • 2007
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