1d8l

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{{Structure
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1d8l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d8l OCA], [http://www.ebi.ac.uk/pdbsum/1d8l PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1d8l RCSB]</span>
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'''E. COLI HOLLIDAY JUNCTION BINDING PROTEIN RUVA NH2 REGION LACKING DOMAIN III'''
'''E. COLI HOLLIDAY JUNCTION BINDING PROTEIN RUVA NH2 REGION LACKING DOMAIN III'''
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[[Category: Nishino, T.]]
[[Category: Nishino, T.]]
[[Category: Shinagawa, H.]]
[[Category: Shinagawa, H.]]
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[[Category: gene regulation]]
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[[Category: Gene regulation]]
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[[Category: helix-hairpin-helix motif]]
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[[Category: Helix-hairpin-helix motif]]
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[[Category: ob-fold]]
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Revision as of 10:34, 2 May 2008

Template:STRUCTURE 1d8l

E. COLI HOLLIDAY JUNCTION BINDING PROTEIN RUVA NH2 REGION LACKING DOMAIN III


Overview

In prokaryotes, RuvA-RuvB complexes play a crucial role in the migration of the Holliday junction, which is a key intermediate of homologous recombination. RuvA binds to the Holliday junction and enhances the ATPase activity of RuvB required for branch migration. RuvA adopts a unique domain structure, which assembles into a tetrameric molecule. The previous mutational and proteolytic analyses suggested that mutations in a carboxyl-terminal domain (domain III) impair binding of RuvA to RuvB. In order to clarify the functional role of each domain in vitro, we established the recombinant expression systems, which allow us to analyze structural and biochemical properties of each domain separately. A small-angle X-ray scattering solution study, combined with X-ray crystallographic analyses, was applied to the tetrameric full-length RuvA and its tetrameric NH2 region (domains I and II) lacking the domain III. These results demonstrated that domain III can be completely separate from the tetrameric major core of the NH2 region and freely mobile in solution, through a remarkably flexible loop. Biochemical analyses indicated that domain III not only interacts with RuvB, but also modulates its ATPase activity. This modulation may facilitate the dynamic coupling between RuvA and RuvB during branch migration.

About this Structure

1D8L is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Modulation of RuvB function by the mobile domain III of the Holliday junction recognition protein RuvA., Nishino T, Iwasaki H, Kataoka M, Ariyoshi M, Fujita T, Shinagawa H, Morikawa K, J Mol Biol. 2000 May 5;298(3):407-16. PMID:10772859 Page seeded by OCA on Fri May 2 13:34:28 2008

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