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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
Author(s) -
Savva Renos,
Pearl Laurence H.
Publication year - 1995
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.340220310
Subject(s) - dna glycosylase , uracil dna glycosylase , uracil , dna , recombinant dna , chemistry , bacteriophage , microbiology and biotechnology , biochemistry , biology , dna repair , escherichia coli , gene
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. © 1995 Wiley‐Liss, Inc.