1uaa
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E. COLI REP HELICASE/DNA COMPLEX
OverviewOverview
Crystal structures of binary and ternary complexes of the E. coli Rep, helicase bound to single-stranded (ss) DNA or ssDNA and ADP were, determined to a resolution of 3.0 A and 3.2 A, respectively. The, asymmetric unit in the crystals contains two Rep monomers differing from, each other by a large reorientation of one of the domains, corresponding, to a swiveling of 130 degrees about a hinge region. Such domain movements, are sufficiently large to suggest that these may be coupled to, translocation of the Rep dimer along DNA. The ssDNA binding site involves, the helicase motifs Ia, III, and V, whereas the ADP binding site involves, helicase motifs I and IV. Residues in motifs II and VI may function to, transduce the allosteric effects of nucleotides on DNA binding. These, structures represent the first view of a DNA helicase bound to DNA.
About this StructureAbout this Structure
1UAA is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
Major domain swiveling revealed by the crystal structures of complexes of E. coli Rep helicase bound to single-stranded DNA and ADP., Korolev S, Hsieh J, Gauss GH, Lohman TM, Waksman G, Cell. 1997 Aug 22;90(4):635-47. PMID:9288744
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