Lindahl M, Svensson L A, Liljas A, Sedelnikova S E, Eliseikina I A, Fomenkova N P, Nevskaya N, Nikonov S V, Garber M B, Muranova T A
Chemical Center, University of Lund, Sweden.
EMBO J. 1994 Mar 15;13(6):1249-54. doi: 10.2210/pdb1ris/pdb.
The amino acid sequence and crystal structure of the ribosomal protein S6 from the small ribosomal subunit of Thermus thermophilus have been determined. S6 is a small protein with 101 amino acid residues. The 3D structure, which was determined to 2.0 A resolution, consists of a four-stranded anti-parallel beta-sheet with two alpha-helices packed on one side. Similar folding patterns have been observed for other ribosomal proteins and may suggest an original RNA-interacting motif. Related topologies are also found in several other nucleic acid-interacting proteins and based on the assumption that the structure of the ribosome was established early in the molecular evolution, the possibility that an ancestral RNA-interacting motif in ribosomal proteins is the evolutionary origin for the nucleic acid-interacting domain in large classes of ribonucleic acid binding proteins should be considered.
嗜热栖热菌小核糖体亚基的核糖体蛋白S6的氨基酸序列和晶体结构已被确定。S6是一种含有101个氨基酸残基的小蛋白。其三维结构的分辨率为2.0埃，由一个四链反平行β折叠片层组成，在一侧堆积有两个α螺旋。其他核糖体蛋白也观察到了类似的折叠模式，这可能暗示了一种原始的RNA相互作用基序。在其他几种与核酸相互作用的蛋白质中也发现了相关的拓扑结构，基于核糖体结构在分子进化早期就已确立的假设，应考虑核糖体蛋白中祖先RNA相互作用基序是一大类核糖核酸结合蛋白中核酸相互作用结构域进化起源的可能性。
