1nt2: Difference between revisions
New page: left|200px<br /><applet load="1nt2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nt2, resolution 2.90Å" /> '''CRYSTAL STRUCTURE OF... |
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[[Image:1nt2.jpg|left|200px]]<br /><applet load="1nt2" size=" | [[Image:1nt2.jpg|left|200px]]<br /><applet load="1nt2" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1nt2, resolution 2.90Å" /> | caption="1nt2, resolution 2.90Å" /> | ||
'''CRYSTAL STRUCTURE OF FIBRILLARIN/NOP5P COMPLEX'''<br /> | '''CRYSTAL STRUCTURE OF FIBRILLARIN/NOP5P COMPLEX'''<br /> | ||
==Overview== | ==Overview== | ||
Nop56p and Nop58p are two core proteins of the box C/D snoRNPs that | 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== | ==About this Structure== | ||
1NT2 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus] with SAM as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | 1NT2 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Archaeoglobus_fulgidus Archaeoglobus fulgidus] with <scene name='pdbligand=SAM:'>SAM</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NT2 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Aittaleb, M.]] | [[Category: Aittaleb, M.]] | ||
[[Category: Chen, Q.]] | [[Category: Chen, Q.]] | ||
[[Category: Daniels, C | [[Category: Daniels, C J.]] | ||
[[Category: Li, H.]] | [[Category: Li, H.]] | ||
[[Category: Palmer, J | [[Category: Palmer, J R.]] | ||
[[Category: Rashid, R.]] | [[Category: Rashid, R.]] | ||
[[Category: SAM]] | [[Category: SAM]] | ||
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[[Category: coiled coil]] | [[Category: coiled coil]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:09:42 2008'' | ||
Revision as of 15:09, 21 February 2008
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CRYSTAL STRUCTURE OF FIBRILLARIN/NOP5P COMPLEX
OverviewOverview
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 StructureAbout this Structure
1NT2 is a Protein complex structure of sequences from Archaeoglobus fulgidus with as ligand. 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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