Purification, crystallization and preliminary X‐ray crystallographic analysis of Rab27a GTPase in complex with exophilin4/Slp2‐a effector | Zendy

Chavas Leonard M. G. | Zendy; Ihara Kentaro | Zendy; Kawasaki Masato | Zendy; Kato Ryuichi | Zendy; Izumi Tetsuro | Zendy; Wakatsuki Soichi | Zendy

Open Access

Purification, crystallization and preliminary X‐ray crystallographic analysis of Rab27a GTPase in complex with exophilin4/Slp2‐a effector

Author(s) -

Chavas Leonard M. G.,

Ihara Kentaro,

Kawasaki Masato,

Kato Ryuichi,

Izumi Tetsuro,

Wakatsuki Soichi

Publication year - 2008

Publication title -

acta crystallographica section f

Language(s) - English

Resource type - Journals

ISSN - 1744-3091

DOI - 10.1107/s1744309108009251

Subject(s) - gtpase , rab , effector , vesicle , biology , exocytosis , gtp' , microbiology and biotechnology , crystallization , membrane , crystallography , biophysics , chemistry , biochemistry , organic chemistry , enzyme

By switching between GTP‐active and GDP‐inactive conformations, small Ras GTPases partly regulate membrane trafficking, cell growth and cytoskeleton dynamics. Among Rab GTPases, the Rab27 subfamily, which comprises Rab27a and Rab27b, controls the proper targeting of secretory vesicles to the plasma membrane. GppNHp‐bound Rab27a in complex with the Rab27‐binding domain of exophilin4/Slp2‐a effector has been purified and crystallized for structural studies. The crystals belong to space group P 2 1 2 1 2 1 and a complete data set was collected to a resolution of 1.8 Å. Eventually, the structural characterization of the Rab27a–exophilin4/Slp2‐a complex will clarify Rab27 recognition by its effectors prior to vesicle tethering and docking.

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