2zub | pdb_00002zub

Left handed RadA

spinqualitylabelsall models 2zub, resolution 2.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2zub is a 2 chain structure with sequence from 'saccharolobus solfataricus'. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 2dfl, 2zuc, 2zud Gene: radA ('Saccharolobus solfataricus') Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [RADA_SULSO] Involved in DNA repair and in homologous recombination. Binds and assemble on single-stranded DNA to form a nucleoprotein filament. Hydrolyzes ATP in a ssDNA-dependent manner and promotes DNA strand exchange between homologous DNA molecules. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed RecA family proteins, including bacterial RecA, archaeal RadA, and eukaryotic Dmc1 and Rad51, mediate homologous recombination, a reaction essential for maintaining genome integrity. In the presence of ATP, these proteins bind a single-strand DNA to form a right-handed nucleoprotein filament, which catalyzes pairing and strand exchange with a homologous double-stranded DNA (dsDNA), by as-yet unknown mechanisms. We recently reported a structure of RadA left-handed helical filament, and here present three new structures of RadA left-handed helical filaments. Comparative structural analysis between different RadA/Rad51 helical filaments reveals that the N-terminal domain (NTD) of RadA/Rad51, implicated in dsDNA binding, is highly flexible. We identify a hinge region between NTD and polymerization motif as responsible for rigid body movement of NTD. Mutant analysis further confirms that structural flexibility of NTD is essential for RadA's recombinase activity. These results support our previous hypothesis that ATP-dependent axial rotation of RadA nucleoprotein helical filament promotes homologous recombination. Three new structures of left-handed RADA helical filaments: structural flexibility of N-terminal domain is critical for recombinase activity.,Chang YW, Ko TP, Lee CD, Chang YC, Lin KA, Chang CS, Wang AH, Wang TF PLoS ONE. 2009;4(3):e4890. Epub 2009 Mar 19. PMID:19295907 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Resolvase

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