Crystal structure of the GAP domain of Gyp1p: first insights into interaction with Ypt/Rab proteins
Crystal structure of the GAP domain of Gyp1p: first insights into interaction with Ypt/Rab proteins
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DOI：
10.1093/emboj/19.19.5105
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发表时间：
2000-10-02
期刊：
影响因子：
11.4
通讯作者：
Scheidig, AJ
中科院分区：
文献类型：
--
作者：
Rak, A;Fedorov, R;Scheidig, AJ
我们展示了Gyp 1 p催化结构域的1.9埃分辨率晶体结构，Gyp 1 p是Ypt蛋白（Rab蛋白的酵母同源物，参与囊泡运输）的特异性GTPase激活蛋白（GAP）。Gyp 1 p是真核生物蛋白质大家族的成员，具有共享的序列基序，以前，没有任何结构信息可用于这类蛋白质的任何成员。Gyp 1 p差距结构域被发现是完全α-螺旋的。然而，观察到的折叠并不与其他α-螺旋GAP重叠，（例如Ras-和Cdc 42/Rho-GAP）。通过突变分析鉴定的保守的和催化关键的精氨酸残基与Ras-和Cdc 42-GAP中的精氨酸指处于可比较的位置，表明Gyp 1 p在差距反应中利用精氨酸指，类似于Ras-和Cdc 42-GAP，Gyp 1 p和Ypt蛋白质之间的相互作用，满足生化数据的模型。
We present the 1.9 Angstrom resolution crystal structure of the catalytic domain of Gyp1p, a specific GTPase activating protein (GAP) for Ypt proteins, the yeast homologues of Rab proteins, which are involved in vesicular transport. Gyp1p is a member of a large family of eukaryotic proteins with shared sequence motifs, Previously, no structural information was available for any member of this class of proteins. The GAP domain of Gyp1p was found to be fully alpha-helical. However, the observed fold does not superimpose with other alpha-helical GAPs (e.g. Ras- and Cdc42/Rho-GAP), The conserved and catalytically crucial arginine residue, identified by mutational analysis, is in a comparable position to the arginine finger in the Ras- and Cdc42-GAPs, suggesting that Gyp1p utilizes an arginine finger in the GAP reaction, in analogy to Ras- and Cdc42-GAPs, A model for the interaction between Gyp1p and the Ypt protein satisfying biochemical data is given.