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    Cloning and expression of the uracil-DNA glycosylase inhibitor (UGI) from bacteriophage PBS-1 and crystallization of a uracil-DNA glycosylase-UGI complex

    Savva, Renos and Pearl, L.H. (1995) Cloning and expression of the uracil-DNA glycosylase inhibitor (UGI) from bacteriophage PBS-1 and crystallization of a uracil-DNA glycosylase-UGI complex. Proteins: Structure, Function, and Bioinformatics 22 (3), pp. 287-289. ISSN 0887-3585.

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    Abstract

    The uracil‐DNA glycosylase inhibitory protein (UGI) from the bacterio‐phage PBS‐l has been cloned and overexpressed. The nucleotide sequence is identical to that for the previously described PBS‐2 inhibitor. The recombinant PBS‐l UGI inhibits the uracil‐DNA glycosylase from herpes simplex virus type‐l (HSV‐l UDGase), and a complex between the HSV‐l UDGase and PBS‐l UGI has been crystallized. The crystals have unit cell dimensions a = 143.21 Å, c = 40.78 Å and are in a polar hexagonal space group. There is a single complex in the asymmetric unit with a solvent content of 62% by volume and the crystals diffract to 2.5Å on a synchrotron radiation source.

    Metadata

    Item Type: Article
    School: School of Science > Biological Sciences
    Research Centres and Institutes: Innovation Management Research, Birkbeck Centre for
    Depositing User: Sarah Hall
    Date Deposited: 14 May 2019 15:22
    Last Modified: 15 Oct 2019 09:03
    URI: https://eprints.bbk.ac.uk/id/eprint/27533

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