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第一类内含子的原子水平结构得以揭示。

Atomic level architecture of group I introns revealed.

作者信息

Vicens Quentin, Cech Thomas R

机构信息

Howard Hughes Medical Institute and Department of Chemistry and Biochemistry, University of Colorado, UCB 215, Boulder, CO 80309-0215, USA.

出版信息

Trends Biochem Sci. 2006 Jan;31(1):41-51. doi: 10.1016/j.tibs.2005.11.008. Epub 2005 Dec 13.

Abstract

Twenty-two years after their discovery as ribozymes, the self-splicing group I introns are finally disclosing their architecture at the atomic level. The crystal structures of three group I introns solved at moderately high resolution (3.1-3.8A) reveal a remarkably conserved catalytic core bound to the metal ions required for activity. The structure of the core is stabilized by an intron-specific set of long-range interactions that involves peripheral elements. Group I intron structures thus provide much awaited and extremely valuable snapshots of how these ribozymes coordinate substrate binding and catalysis.

摘要

在被发现为核酶22年后,自我剪接的I组内含子终于在原子水平上揭示了其结构。三个I组内含子在中等高分辨率(3.1 - 3.8埃)下解析出的晶体结构显示,一个与活性所需金属离子结合的高度保守的催化核心。核心结构通过一组涉及周边元件的内含子特异性长程相互作用得以稳定。因此,I组内含子结构提供了这些核酶如何协调底物结合和催化作用的期待已久且极其有价值的瞬间图像。

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