1W94

Crystal Structure of Mil (Mth680), an archaeal Imp4-like protein

1W94 の概要

• エントリーDOI: 10.2210/pdb1w94/pdb
• 分子名称: PROBABLE BRIX-DOMAIN RIBOSOMAL BIOGENESIS PROTEIN (2 entities in total)
• 機能のキーワード: archaeal imp4-brix domain, imp4 domain, brix domain, rna-binding protein
• 由来する生物種: METHANOTHERMOBACTER THERMAUTOTROPHICUS
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 36183.23

構造登録者

Ng, C.L.,Antson, A.A.,Ortiz-Lombardia, M. (登録日: 2004-10-06, 公開日: 2005-01-19, 最終更新日: 2024-10-16)

主引用文献

Ng, C.L.,Waterman, D.,Koonin, E.V.,Antson, A.A.,Ortiz-Lombardia, M.
Crystal Structure of Mil (Mth680): Internal Duplication and Similarity between the Imp4/Brix Domain and the Anticodon-Binding Domain of Class Iia Aminoacyl-tRNA Synthetases
Embo Rep., 6:140-, 2005

PubMed Abstract: Proteins of the Imp4/Brix superfamily are involved in ribosomal RNA processing, an essential function in all cells. We report the first structure of an Imp4/Brix superfamily protein, the Mil (for Methanothermobacter thermautotrophicus Imp4-like) protein (gene product Mth680), from the archaeon M. thermautotrophicus. The amino- and carboxy-terminal halves of Mil show significant structural similarity to one another, suggesting an origin by means of an ancestral duplication. Both halves show the same fold as the anticodon-binding domain of class IIa aminoacyl-tRNA synthetases, with greater conservation seen in the N-terminal half. This structural similarity, together with the charge distribution in Mil, suggests that Imp4/Brix superfamily proteins could bind single-stranded segments of RNA along a concave surface formed by the N-terminal half of their beta-sheet and a central alpha-helix. The crystal structure of Mil is incompatible with the presence, in the Imp4/Brix domain, of a helix-turn-helix motif that was proposed to comprise the RNA-binding moiety of the Imp4/Brix proteins.

PubMed: 15654320
DOI: 10.1038/SJ.EMBOR.7400328

実験手法

X-RAY DIFFRACTION (2 Å)