1nt2: Difference between revisions

Revision as of 17:11, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1nt2.png

Template:STRUCTURE 1nt2

CRYSTAL STRUCTURE OF FIBRILLARIN/NOP5P COMPLEXCRYSTAL STRUCTURE OF FIBRILLARIN/NOP5P COMPLEX

Template:ABSTRACT PUBMED 12598892

About this StructureAbout this Structure

1NT2 is a Protein complex structure of sequences from Archaeoglobus fulgidus. Full crystallographic information is available from OCA.

ReferenceReference

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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OCA

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-'''CRYSTAL STRUCTURE OF FIBRILLARIN/NOP5P COMPLEX'''
+===CRYSTAL STRUCTURE OF FIBRILLARIN/NOP5P COMPLEX===
-==Overview==
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-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.
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