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

被引：3

作者：

Chavas, Leonard M. G. ^{[1
,2
]}

Ihara, Kentaro ^{[2
]}

Kawasaki, Masato ^{[2
]}

Kato, Ryuichi ^{[2
]}

Izumi, Tetsuro ^{[3
]}

Wakatsuki, Soichi ^{[2
]}

机构：

[1] Univ Manchester, Fac Life Sci, Oxford, England

[2] High Energy Accelerator Res Org, Inst Mat Struct Sci, Struct Biol Res Ctr, Photon Factory, Tsukuba, Ibaraki 3050801, Japan

[3] Gunma Univ, Inst Mol & Cellular Regulat, Dept Mol Med, Maebashi, Gunma 3718512, Japan

来源：

ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2008年 / 64卷

关键词：

D O I：

10.1107/S1744309108009251

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

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 P2(1)2(1)2(1) and a complete data set was collected to a resolution of 1.8 angstrom. Eventually, the structural characterization of the Rab27a-exophilin4/Slp2-a complex will clarify Rab27 recognition by its effectors prior to vesicle tethering and docking.

引用

页码：599 / 601

页数：3

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