1nt2

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{{STRUCTURE_1nt2| PDB=1nt2 | SCENE= }}
{{STRUCTURE_1nt2| PDB=1nt2 | SCENE= }}
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'''CRYSTAL STRUCTURE OF FIBRILLARIN/NOP5P COMPLEX'''
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===CRYSTAL STRUCTURE OF FIBRILLARIN/NOP5P COMPLEX===
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==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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(as it appears on PubMed at http://www.pubmed.gov), where 12598892 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12598892}}
==About this Structure==
==About this Structure==
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[[Category: Binding motif]]
[[Category: Binding motif]]
[[Category: Coiled coil]]
[[Category: Coiled coil]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:56:39 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 17:11:31 2008''

Revision as of 14:11, 27 July 2008

Template:STRUCTURE 1nt2

CRYSTAL STRUCTURE OF FIBRILLARIN/NOP5P COMPLEX

Template:ABSTRACT PUBMED 12598892

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

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