Structural analyses of peptide release factor 1 from Thermotoga maritima reveal domain flexibility required for its interaction with the ribosome
Structural analyses of peptide release factor 1 from Thermotoga maritima reveal domain flexibility required for its interaction with the ribosome
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DOI：
10.1016/j.jmb.2004.05.055
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发表时间：
2004-07-30
影响因子：
5.6
通讯作者：
Kim, SH
中科院分区：
文献类型：
--
作者：
Shin, DH;Brandsen, J;Kim, SH
用硒代蛋氨酸单波长反常色散（SAD）技术测定了海栖热袍菌（Thermotoga maritima，gi 4981173）肽链释放因子1（RF 1）的晶体结构，其分辨率为2.65埃。RF 1是一种识别终止密码子并促进核糖体上tRNA释放新生多肽的蛋白质。硒代蛋氨酸标记的RF 1在空间群P2（1）中结晶，每个不对称单元有三个单体。它的尺寸约为75 A x 70 A x 45 A，由四个域组成。每个RF 1结构域的整体折叠显示出与大肠杆菌RF 2几乎相同的拓扑结构，除了RF 1的N-末端结构域比RF 2的短，C-末端结构域比RF 2的长。RM的N-末端结构域表明相对于RF 2的N-末端结构域具有近似90度的角度的刚体运动。包括这些特征，RF 1具有三肽反密码子PVT基序而不是RF 2的SPF基序，这赋予了对终止密码子的特异性。在不对称单元中的三个分子的分析和与RF 2的比较揭示了结构域I和III的动态运动的存在，所述结构域I和III通过铰链环锚定到中心结构域。RF 1的晶体结构阐明了这个家族的固有特性，即具有大的结构域运动，以便与核糖体一起发挥适当的功能。(C)2004爱思唯尔有限公司保留所有权利。
We have determined the crystal structure of peptide chain release factor 1 (RF1) from Thermotoga maritima (gi 4981173) at 2.65 Angstrom resolution by selenomethionine single-wavelength anomalous dispersion (SAD) techniques. RF1 is a protein that recognizes stop codons and promotes the release of a nascent polypeptide from tRNA on the ribosome. Selenomethionine-labeled RF1 crystallized in space group P2(1) with three monomers per asymmetric unit. It has approximate dimensions of 75 A x 70 A x 45 A and is composed of four domains. The overall fold of each RF1 domain shows almost the same topology with Escherichia coli RF2, except that the RF1 N-terminal domain is shorter and the C-terminal domain is longer than that of RF2. The N-terminal domain of RM indicates a rigid-body movement relative to that of RF2 with an angle of similar to 90degrees. Including these features, RF1 has a tripeptide anticodon PVT motif instead of the SPF motif of RF2, which confers the specificity towards the stop codons. The analyses of three molecules in the asymmetric unit and comparison with RF2 revealed the presence of dynamic movement of domains I and III, which are anchored to the central domain by hinge loops. The crystal structure of RF1 elucidates the intrinsic property of this family of having large domain movements for proper function with the ribosome. (C) 2004 Elsevier Ltd. All rights reserved.