The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution
The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution
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DOI：
10.1126/science.289.5481.905
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发表时间：
2000-08-11
期刊：
影响因子：
56.9
通讯作者：
Steitz, TA
中科院分区：
文献类型：
--
作者：
Ban, N;Nissen, P;Steitz, TA
核糖体大亚基催化肽键形成并结合起始、终止和延伸因子。我们在2.4埃的分辨率下测定了海生盐球藻核糖体大亚基的晶体结构，包括该亚基3045个核苷酸中的2833个和31个蛋白质中的27个。它的RNA结构域都有不规则的形状并在核糖体中组合在一起就像三维拼图的碎片形成一个巨大的整体结构。蛋白质在其表面的任何地方都是丰富的，除了在活性位点，在那里发生肽键形成和它接触的小亚基。大多数蛋白质通过与几个RNA结构域相互作用来稳定结构，通常使用特异性折叠延伸进入亚基的内部。
The large ribosomal subunit catalyzes peptide bond formation and binds initiation, termination, and elongation factors. We have determined the crystal structure of the Large ribosomal subunit from Haloarcula marismortui at 2.4 angstrom resolution, and it includes 2833 of the subunit's 3045 nucleotides and 27 of its 31 proteins. The domains of its RNAs all have irregular shapes and fit together in the ribosome Like the pieces of a three-dimensional jigsaw puzzle to form a Large, monolithic structure. Proteins are abundant everywhere on its surface except in the active site where peptide bond formation occurs and where it contacts the small subunit. Most of the proteins stabilize the structure by interacting with several RNA domains, often using idiosyncratically folded extensions that reach into the subunit's interior.