1nt2
From Proteopedia
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CRYSTAL STRUCTURE OF FIBRILLARIN/NOP5P COMPLEX
Overview
Nop56p and Nop58p are two core proteins of the box C/D snoRNPs that, interact concurrently with fibrillarin and snoRNAs to function in enzyme, assembly and catalysis. Here we report the 2.9 A resolution co-crystal, structure of an archaeal homolog of Nop56p/Nop58p, Nop5p, in complex with, fibrillarin from Archaeoglobus fulgidus (AF) and the methyl donor, S-adenosyl-L-methionine. The N-terminal domain of Nop5p forms a, complementary surface to fibrillarin that serves to anchor the catalytic, subunit and to stabilize cofactor binding. A coiled coil in Nop5p mediates, dimerization of two fibrillarin-Nop5p heterodimers for optimal, interactions with bipartite box C/D RNAs. Structural analysis and, complementary biochemical data demonstrate that the conserved C-terminal, domain of Nop5p harbors RNA-binding sites. A model of box C/D snoRNP, assembly is proposed based on the presented structural and biochemical, data.
About this Structure
1NT2 is a Protein complex structure of sequences from Archaeoglobus fulgidus with SAM as ligand. Full crystallographic information is available from OCA.
Reference
Structure and function of archaeal box C/D sRNP core proteins., Aittaleb M, Rashid R, Chen Q, Palmer JR, Daniels CJ, Li H, Nat Struct Biol. 2003 Apr;10(4):256-63. PMID:12598892
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