2nnw
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= flpA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2261 Pyrococcus furiosus]) | |GENE= flpA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2261 Pyrococcus furiosus]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2nnw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nnw OCA], [http://www.ebi.ac.uk/pdbsum/2nnw PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2nnw RCSB]</span> | ||
}} | }} | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:05:44 2008'' |
Revision as of 01:05, 31 March 2008
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| , resolution 2.7Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | flpA (Pyrococcus furiosus) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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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