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.
journal_name
EMBO Repjournal_title
EMBO reportsauthors
Ng CL,Waterman D,Koonin EV,Antson AA,Ortiz-Lombardía Mdoi
10.1038/sj.embor.7400328keywords:
subject
Has Abstractpub_date
2005-02-01 00:00:00pages
140-6issue
2eissn
1469-221Xissn
1469-3178pii
7400328journal_volume
6pub_type
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