Crystal structure of the site-specific recombinase gamma delta resolvase complexed with a 34 bp cleavage site
Article Abstract:
The structure of gama delta resolvase with a 34 bp substrate DNA, when calculated at 3.0 angstrom resolution shows a sharp inclination by 60 degrees at the recombination crossover point towards the main groove and away from the resolvase catalytic domains. The C-terminal of one-third of resolvase, disorganized without DNA, creates an arm and a 3-helix DNA-binding field on the reverse side of the DNA from the N-terminal field. The arms surround the minor groove of the central 16 bp, and the DNA-binding areas touch the major grooves near the outermost boundaries of the binding area.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1995
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Crystal structure and ATPase activity of MutL: implications for DNA repair and mutagenesis
Article Abstract:
A crystal structure of the N-terminal region of of E. coli MutL or LN40 that binds to DNA and can induce MutH in DNA repair is described. MutL is an ATPase and that ATP binding activates conformational changes in MutL. Furthermore, the ATP-dependent conformational changes regulate interactions of MutL with other components in the DNA repair mechanism. Based on these analyses, it is suggested that MutL influences ATP to regulate interactions among MutS, MutH, and UvrD and to coordinate processes in DNA mismatch repair.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1998
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Crystal structure of a Y-family DNA polymerase in action: a mechanism for error-prone and lesion-bypass replication
Article Abstract:
The molecular basis of the low-fidelity DNA synthesis and traverse replication-blocking lesions in DNA is due to P2 DNA polymerase IV making limited and nonspecific contacts with the replicating DNA base pair and translocating two template bases simultaneously to the active site.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 2001
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