1ugh
From Proteopedia
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CRYSTAL STRUCTURE OF HUMAN URACIL-DNA GLYCOSYLASE IN COMPLEX WITH A PROTEIN INHIBITOR: PROTEIN MIMICRY OF DNA
Contents |
Overview
Uracil-DNA glycosylase inhibitor (Ugi) is a B. subtilis bacteriophage, protein that protects the uracil-containing phage DNA by irreversibly, inhibiting the key DNA repair enzyme uracil-DNA glycosylase (UDG). The 1.9, A crystal structure of Ugi complexed to human UDG reveals that the Ugi, structure, consisting of a twisted five-stranded antiparallel beta sheet, and two alpha helices, binds by inserting a beta strand into the conserved, DNA-binding groove of the enzyme without contacting the uracil specificity, pocket. The resulting interface, which buries over 1200 A2 on Ugi and, involves the entire beta sheet and an alpha helix, is polar and contains, 22 water molecules. Ugi binds the sequence-conserved DNA-binding groove of, UDG via shape and electrostatic complementarity, specific charged hydrogen, bonds, and hydrophobic packing enveloping Leu-272 from a protruding UDG, loop. The apparent mimicry by Ugi of DNA interactions with UDG provides, both a structural mechanism for UDG binding to DNA, including the, enzyme-assisted expulsion of uracil from the DNA helix, and a, crystallographic basis for the design of inhibitors with scientific and, therapeutic applications.
Disease
Known diseases associated with this structure: Immunodeficiency with hyper IgM, type 4 OMIM:[191525]
About this Structure
1UGH is a Protein complex structure of sequences from Homo sapiens and Phage pbs1. Active as Uridine nucleosidase, with EC number 3.2.2.3 Full crystallographic information is available from OCA.
Reference
Crystal structure of human uracil-DNA glycosylase in complex with a protein inhibitor: protein mimicry of DNA., Mol CD, Arvai AS, Sanderson RJ, Slupphaug G, Kavli B, Krokan HE, Mosbaugh DW, Tainer JA, Cell. 1995 Sep 8;82(5):701-8. PMID:7671300
Page seeded by OCA on Fri Feb 15 17:02:10 2008
