1nt2: Difference between revisions
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'''CRYSTAL STRUCTURE OF FIBRILLARIN/NOP5P COMPLEX''' | '''CRYSTAL STRUCTURE OF FIBRILLARIN/NOP5P COMPLEX''' | ||
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[[Category: Palmer, J R.]] | [[Category: Palmer, J R.]] | ||
[[Category: Rashid, R.]] | [[Category: Rashid, R.]] | ||
[[Category: | [[Category: Ademet]] | ||
[[Category: | [[Category: Binding motif]] | ||
[[Category: | [[Category: Coiled coil]] | ||
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Revision as of 23:56, 2 May 2008
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. 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 Page seeded by OCA on Sat May 3 02:56:39 2008