2nnw

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'''Alternative conformations of Nop56/58-fibrillarin complex and implication for induced-fit assenly of box C/D RNPs'''<br />
'''Alternative conformations of Nop56/58-fibrillarin complex and implication for induced-fit assenly of box C/D RNPs'''<br />
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==About this Structure==
==About this Structure==
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2NNW is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2NNW OCA].
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2NNW is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Pyrococcus_furiosus Pyrococcus furiosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NNW OCA].
==Reference==
==Reference==
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[[Category: transferase]]
[[Category: transferase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 12:48:42 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 14:01:17 2008''

Revision as of 12:01, 23 January 2008


2nnw, resolution 2.7Å

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Alternative conformations of Nop56/58-fibrillarin complex and implication for induced-fit assenly of box C/D RNPs

Overview

The Nop56/58-fibrillarin heterocomplex is a core protein complex of the, box C/D ribonucleoprotein particles that modify and process ribosomal, RNAs. The previous crystal structure of the Archaeoglobus fulgidus complex, revealed a symmetric dimer of two Nop56/58-fibrillarin complexes linked by, the coiled-coil domains of the Nop56/68 proteins. However, because the A., fulgidus Nop56/58 protein lacks some domains found in most other species, it was thought that the bipartite architecture of the heterocomplex was, not likely a general phenomenon. Here we report the crystal structure of, the Nop56/58-fibrillarin complex bound with methylation cofactor, S-adenosyl-L-methionine from Pyrococcus furiosus, at 2.7 A. The new, complex confirms the generality of the previously observed bipartite, arrangement. In addition however, the conformation of Nop56/58 in the new, structure differs substantially from that in the earlier structure. The, distinct conformations of Nop56/58 suggest potential flexibility in, Nop56/58. Computational normal mode analysis supports this view., Importantly, fibrillarin is repositioned within the two complexes. We, propose that hinge motion within Nop56/58 has important implications for, the possibility of simultaneously positioning two catalytic sites at the, two target sites of a bipartite box C/D guide RNA.

About this Structure

2NNW is a Protein complex structure of sequences from Pyrococcus furiosus. Full crystallographic information is available from OCA.

Reference

Alternative Conformations of the Archaeal Nop56/58-Fibrillarin Complex Imply Flexibility in Box C/D RNPs., Oruganti S, Zhang Y, Li H, Robinson H, Terns MP, Terns RM, Yang W, Li H, J Mol Biol. 2007 Aug 31;371(5):1141-50. Epub 2007 Jun 15. PMID:17617422

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