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