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  • 1
    ISSN: 1545-9985
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Medicine
    Notes: [Auszug] The bacterial septum-located DNA translocase FtsK coordinates circular chromosome segregation with cell division. Rapid translocation of DNA by FtsK is directed by 8-base-pair DNA motifs (KOPS), so that newly replicated termini are brought together at the developing septum, thereby facilitating ...
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Copenhagen : International Union of Crystallography (IUCr)
    Acta crystallographica 57 (2001), S. 469-471 
    ISSN: 1399-0047
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Notes: A protein belonging to the Lrp/AsnC transcription-factor family, pot1216151, from the hyperthermophilic archaeon Pyrococcus sp. OT3 was crystallized. In Escherichia coli, leucine-responsive protein (Lrp) and AsnC regulate a number of metabolic genes. The crystals of pot1216151 diffracted to 2.3 Å using a conventional X-ray source and to 1.8 Å using a synchrotron-radiation source. The space group was identified to be P3121 or P3221, with unit-cell parameters a = b = 96.9, c = 98.5 Å. In combination with diffraction data obtained from K2[Pt(CN)6] and K(AuCl4) derivatives, an electron-density map was calculated at a resolution of 3.0 Å. Four monomers were identified in the asymmetric unit, with four β-strands and two α-helices in each monomer.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    New York : Wiley-Blackwell
    Biopolymers 44 (1997), S. 335-359 
    ISSN: 0006-3525
    Keywords: DNA recognition ; β-sheet ; DNA-protein interaction ; dinucleotide parameter ; major groove ; minor groove ; Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The modes of DNA recognition by β-sheets are analyzed by using the known crystal and solution three-dimensional structures of DNA-protein complexes. Close fitting of the protein surface and the DNA surface determines the binding geometry. Interaction takes place so that essentially the N-to-C direction of the β-strands either follows or crosses the DNA groove. Upon following the major groove a two-stranded antiparallel β-sheet dives into the groove and contacts DNA bases with its convex side facing the DNA, while upon following the minor groove, it binds around the sugar-phosphate backbones, with its opposite concave side shielding the DNA. In order for the β-strands crossing the minor groove to interact with the DNA, the dinucleotide steps need to almost totally helically untwist and roll around major groove. The β-sheet, on the other hand, needs to adopt a concave curvature on the binding surface in the direction that follows the DNA minor groove, and a convex surface in the direction that bridges the sugar-phosphate backbones across the groove. The result is to produce a hyperbolic paraboloidal DNA-binding surface. © 1998 John Wiley & Sons, Inc. Biopoly 44: 335-359, 1997
    Additional Material: 16 Ill.
    Type of Medium: Electronic Resource
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