1NT2

CRYSTAL STRUCTURE OF FIBRILLARIN/NOP5P COMPLEX

Summary for 1NT2

• Entry DOI: 10.2210/pdb1nt2/pdb
• Related: 1FBN
• Descriptor: Fibrillarin-like pre-rRNA processing protein, conserved hypothetical protein, S-ADENOSYLMETHIONINE (3 entities in total)
• Functional Keywords: ademet, binding motif, rna binding protein
• Biological source: Archaeoglobus fulgidus; More
• Total number of polymer chains: 2
• Total formula weight: 54857.11

Authors

Aittaleb, M.,Rashid, R.,Chen, Q.,Palmer, J.R.,Daniels, C.J.,Li, H. (deposition date: 2003-01-28, release date: 2003-04-01, Last modification date: 2024-02-14)

Primary citation

Aittaleb, M.,Rashid, R.,Chen, Q.,Palmer, J.R.,Daniels, C.J.,Li, H.
Structure and function of archaeal box C/D sRNP core proteins.
Nat.Struct.Biol., 10:256-263, 2003

PubMed Abstract: 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.

PubMed: 12598892
DOI: 10.1038/nsb905

Experimental method

X-RAY DIFFRACTION (2.9 Å)