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Molecular mechanism of constitutively active Rab11A was revealed by crystal structure of Rab11A S20V

Jae Young Choi1, Young-Cheul Shin2, Jong Hwan Yoon1

  • 1School of Biotechnology and Graduate School of Biochemistry at Yeungnam University, Gyeongsan, South Korea.

FEBS Letters
|February 17, 2016
PubMed

Rab11A is a small GTP-binding protein involved in the regulation of vesicle trafficking during recycling of endosomes. Substitution of S20 to V (S20V) at Rab11A inhibits the GTP hydrolysis activity of Rab11A. This mutation is known to be constitutively in an active form. Here, we report the crystal structure of the human Rab11A S20V mutant form complexed with GTP at a resolution of 2.4 Å. Without adding any substrate, Rab11A contained non-hydrolyzed natural substrate GTP in the nucleotide binding pocket with Mg(2+). In our observations, substituted V20 of Rab11A was found to interfere with proper localization of the water molecule, which mediated GTP hydrolysis, resulting in GTP being locked in an active form of Rab11A S20V.

Keywords:
Rab11crystal structuremembrane traffickingsmall G protein

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