2c9o

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[[Image:2c9o.gif|left|200px]]
[[Image:2c9o.gif|left|200px]]
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{{Structure
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|PDB= 2c9o |SIZE=350|CAPTION= <scene name='initialview01'>2c9o</scene>, resolution 2.20&Aring;
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The line below this paragraph, containing "STRUCTURE_2c9o", creates the "Structure Box" on the page.
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{{STRUCTURE_2c9o| PDB=2c9o | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2c9o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c9o OCA], [http://www.ebi.ac.uk/pdbsum/2c9o PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2c9o RCSB]</span>
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'''3D STRUCTURE OF THE HUMAN RUVB-LIKE HELICASE RUVBL1'''
'''3D STRUCTURE OF THE HUMAN RUVB-LIKE HELICASE RUVBL1'''
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[[Category: Gorynia, S.]]
[[Category: Gorynia, S.]]
[[Category: Matias, P M.]]
[[Category: Matias, P M.]]
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[[Category: aaa+-atpase]]
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[[Category: Aaa+-atpase]]
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[[Category: activator]]
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[[Category: Activator]]
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[[Category: atp-binding]]
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[[Category: Atp-binding]]
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[[Category: Chromatin regulator]]
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[[Category: dna recombination]]
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[[Category: helicase]]
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[[Category: Helicase]]
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[[Category: hexameric helicase]]
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[[Category: Hexameric helicase]]
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[[Category: hydrolase]]
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[[Category: Hydrolase]]
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[[Category: nuclear protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 21:31:12 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:18:30 2008''
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Revision as of 18:31, 3 May 2008

Image:2c9o.gif

Template:STRUCTURE 2c9o

3D STRUCTURE OF THE HUMAN RUVB-LIKE HELICASE RUVBL1


Overview

RuvBL1 is an evolutionarily highly conserved eukaryotic protein belonging to the AAA(+)-family of ATPases (ATPase associated with diverse cellular activities). It plays important roles in essential signaling pathways such as the c-Myc and Wnt pathways in chromatin remodeling, transcriptional and developmental regulation, and DNA repair and apoptosis. Herein we present the three-dimensional structure of the selenomethionine variant of human RuvBL1 refined using diffraction data to 2.2A of resolution. The crystal structure of the hexamer is formed of ADP-bound RuvBL1 monomers. The monomers contain three domains, of which the first and the third are involved in ATP binding and hydrolysis. Although it has been shown that ATPase activity of RuvBL1 is needed for several in vivo functions, we could only detect a marginal activity with the purified protein. Structural homology and DNA binding studies demonstrate that the second domain, which is unique among AAA(+) proteins and not present in the bacterial homolog RuvB, is a novel DNA/RNA-binding domain. We were able to demonstrate that RuvBL1 interacted with single-stranded DNA/RNA and double-stranded DNA. The structure of the RuvBL1.ADP complex, combined with our biochemical results, suggest that although RuvBL1 has all the structural characteristics of a molecular motor, even of an ATP-driven helicase, one or more as yet undetermined cofactors are needed for its enzymatic activity.

About this Structure

2C9O is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of the human AAA+ protein RuvBL1., Matias PM, Gorynia S, Donner P, Carrondo MA, J Biol Chem. 2006 Dec 15;281(50):38918-29. Epub 2006 Oct 23. PMID:17060327 Page seeded by OCA on Sat May 3 21:31:12 2008

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