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Journal Article

Rab-subfamily-specific regions of Ypt7p are structurally different from other RabGTPases

MPS-Authors

Constantinescu,  Alexandru-Tudor
Max Planck Institute of Molecular Physiology, Max Planck Society;

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Rak,  Alexey
Abt. III: Physikalische Biochemie, Max Planck Institute of Molecular Physiology, Max Planck Society;

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Alexandrov,  Kirill
Abt. III: Physikalische Biochemie, Max Planck Institute of Molecular Physiology, Max Planck Society;

Esters,  Heike
Max Planck Institute of Molecular Physiology, Max Planck Society;

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Goody,  Roger S.
Abt. III: Physikalische Biochemie, Max Planck Institute of Molecular Physiology, Max Planck Society;

/persons/resource/persons98725

Scheidig,  Axel Jörg
Abt. III: Physikalische Biochemie, Max Planck Institute of Molecular Physiology, Max Planck Society;

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Citation

Constantinescu, A.-T., Rak, A., Alexandrov, K., Esters, H., Goody, R. S., & Scheidig, A. J. (2002). Rab-subfamily-specific regions of Ypt7p are structurally different from other RabGTPases. Structure, 10(4): 1, pp. 569-579. Retrieved from http://dx.doi.org/10.1016/S0969-2126(02)00737-2.


Cite as: https://hdl.handle.net/11858/00-001M-0000-0014-0EA6-7
Abstract
The GTPase Ypt7p from S. cerevisiae is involved in late endosome-to-vacuole transport and homotypic vacuole fusion. We present crystal structures of the GDP- and GppNHp-bound conformation of Ypt7p solved at 1.35 and 1.6 Angstrom resolution, respectively. Despite the similarity of the overall structure to other Ypt/Rab proteins, Ypt7p displays small but significant differences. The Ypt7p-specific residues Tyr33 and Tyr37 cause a difference in the main chain trace of the RabSF2 region and form a characteristic surface epitope, Ypt7p(.)GppNHp does not display the helix alpha2, characteristic of the Ras-superfamily, but instead possess an extended loop L4/L5. Due to insertions in loops L3 and L7, the neighboring RabSF1 and RabSF4 regions are different in their conformations to those of other Ypt/Rab proteins.