1nt2

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(New page: 200px<br /><applet load="1nt2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nt2, resolution 2.90&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1nt2.jpg|left|200px]]<br /><applet load="1nt2" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1nt2.jpg|left|200px]]<br /><applet load="1nt2" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1nt2, resolution 2.90&Aring;" />
caption="1nt2, resolution 2.90&Aring;" />
'''CRYSTAL STRUCTURE OF FIBRILLARIN/NOP5P COMPLEX'''<br />
'''CRYSTAL STRUCTURE OF FIBRILLARIN/NOP5P COMPLEX'''<br />
==Overview==
==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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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==
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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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NT2 OCA].
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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.]]
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[[Category: Daniels, C.J.]]
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[[Category: Daniels, C J.]]
[[Category: Li, H.]]
[[Category: Li, H.]]
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[[Category: Palmer, J.R.]]
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[[Category: Palmer, J R.]]
[[Category: Rashid, R.]]
[[Category: Rashid, R.]]
[[Category: SAM]]
[[Category: SAM]]
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[[Category: coiled coil]]
[[Category: coiled coil]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:31:56 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:09:42 2008''

Revision as of 12:09, 21 February 2008


1nt2, resolution 2.90Å

Drag the structure with the mouse to rotate

CRYSTAL STRUCTURE OF FIBRILLARIN/NOP5P COMPLEX

Overview

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

1NT2 is a Protein complex structure of sequences from Archaeoglobus fulgidus with as ligand. 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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