Structure and dynamics of γ-SNAP:: Insight into flexibility of proteins from the SNAP family
Structure and dynamics of γ-SNAP:: Insight into flexibility of proteins from the SNAP family
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DOI：
10.1002/prot.21468
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发表时间：
2008-01-01
影响因子：
2.9
通讯作者：
Phillips, George N., Jr.
中科院分区：
文献类型：
--
作者：
Bitto, Eduard;Bingman, Craig A.;Phillips, George N., Jr.
可溶性N-乙基马来酰亚胺敏感因子附着蛋白γ（Soluble N-ethylmaleimide-sensitive factor attachment protein gamma，γ-SNAP）是参与细胞内膜运输的真核蛋白家族成员。斑马鱼γ-SNAP的X射线结构被确定为2.6埃，并揭示了一种全螺旋蛋白质，该蛋白质由螺旋发夹的延伸扭曲片层组成，其羧基末端具有螺旋束结构域。分析了多个观察到的γ-SNAP分子和Sec 17（来自酵母的SNAP家族蛋白）之间的结构和构象差异。γ-SNAP分子的构象变化与结构的两个最低频率正常模式非常精确地匹配。从γ-SNAP和Sec 17的最低频率模式的比较表明，结构共享的灵活性的首选方向，对应于弯曲和扭曲的扭曲片图案。我们讨论了SNAP受体回收过程中20 S复合物解体机制的SNAP蛋白的灵活性相关的可能后果。
Soluble N-ethylmaleimide-sensitive factor attachment protein gamma (gamma-SNAP) is a member Of an eukaryotic Protein family involved in intracellular membrane trafficking. The X-ray structure of Brachydanio rerio gamma-SNAP was determined to 2.6 angstrom and revealed an all-helical protein comprised of an extended twisted-sheet of helical hairpins with a helical-bundle domain on its carboxy-terminal end. Structural and conformational differences between multiple observed gamma-SNAP molecules and Sec17, a SNAP family protein from yeast, are analyzed. Conformational variation in gamma-SNAP molecules is matched with great precision by the two lowest frequency normal modes of the structure. Comparison of the lowest-frequency modes from gamma-SNAP and Sec17 indicated that the structures share preferred directions of flexibility, corresponding to bending and twisting of the twisted sheet motif. We discuss possible consequences related to the flexibility of the SNAP proteins for the mechanism of the 20S complex disassembly during the SNAP receptors recycling.