2nnw

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
[[Image:2nnw.jpg|left|200px]]
[[Image:2nnw.jpg|left|200px]]
-
{{Structure
+
<!--
-
|PDB= 2nnw |SIZE=350|CAPTION= <scene name='initialview01'>2nnw</scene>, resolution 2.7&Aring;
+
The line below this paragraph, containing "STRUCTURE_2nnw", creates the "Structure Box" on the page.
-
|SITE=
+
You may change the PDB parameter (which sets the PDB file loaded into the applet)
-
|LIGAND=
+
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-
|ACTIVITY=
+
or leave the SCENE parameter empty for the default display.
-
|GENE= flpA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2261 Pyrococcus furiosus])
+
-->
-
|DOMAIN=
+
{{STRUCTURE_2nnw| PDB=2nnw | SCENE= }}
-
|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>
+
-
}}
+
'''Alternative conformations of Nop56/58-fibrillarin complex and implication for induced-fit assenly of box C/D RNPs'''
'''Alternative conformations of Nop56/58-fibrillarin complex and implication for induced-fit assenly of box C/D RNPs'''
Line 30: Line 27:
[[Category: Terns, R.]]
[[Category: Terns, R.]]
[[Category: Zhang, Y.]]
[[Category: Zhang, Y.]]
-
[[Category: box c/d]]
+
[[Category: Box c/d]]
-
[[Category: transferase]]
+
[[Category: Transferase]]
-
 
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 09:41:08 2008''
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:05:44 2008''
+

Revision as of 06:41, 4 May 2008

Template:STRUCTURE 2nnw

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 Page seeded by OCA on Sun May 4 09:41:08 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools