10DA

Crystal structure of Pyrobaculum islandicum L7Ae

10DA の概要

• エントリーDOI: 10.2210/pdb10da/pdb
• 分子名称: Large ribosomal subunit protein eL8, SODIUM ION, 1,2-ETHANEDIOL, ... (5 entities in total)
• 機能のキーワード: rnase p t type archaeal, rna binding protein
• 由来する生物種: Pyrobaculum islandicum
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 66251.92

構造登録者

Chan, C.W.,Mondragon, A. (登録日: 2026-01-13, 公開日: 2026-08-26)

主引用文献

Chan, C.W.,Mondragon, A.
Crystal structures of type T archaeal ribonuclease P Rpp30, Rpp30/Pop5, and L7Ae provide insights into a reduced RNase P.
Nucleic Acids Res., 54:-, 2026

PubMed Abstract: RNase P is primarily responsible for processing the 5' end of precursor transfer RNA (tRNA). Although there are protein-only RNase P enzymes, the most widely distributed RNase Ps form ribonucleoprotein complexes where the number of protein components varies across evolutionary domains. Ribonucleoprotein RNase P enzymes universally contain a single RNA component. Pyrobaculum, a genus of archaeal hyperthermophiles, possess a minimal RNase P composed of a small RNA subunit and four small proteins. To understand the structure of this minimal RNase P, high-resolution structures of three protein components from Pyrobaculum were determined. These structures reveal that the proteins closely resemble their larger homologs, although entire secondary structure elements are absent in some instances. Modeling of the RNA subunit suggests a structure closely related to the RNA components of other RNase P complexes, but with a minimal S-domain containing only a single T-loop. The modeling further supports the formation of an RNase P complex that retains all the elements needed for tRNA recognition and processing. Finally, RNA composition analysis by size exclusion chromatography indicates that the L7Ae protein component may assist in the folding and structural stabilization of the RNA subunit.

PubMed: 42581760
DOI: 10.1093/nar/gkag792

実験手法

X-RAY DIFFRACTION (0.998 Å)