deCODE biostructures Reveals Structure of a new Antibiotic Drug Target
News Jan 06, 2009
deCODE biostructures announces that they have elucidated the three-dimensional structure of an enzyme needed for DNA replication in Gram-positive bacteria.
Research published in the Proceedings of the National Academy of Sciences of the United States of America, entitled “Structure of PolC Reveals Unique DNA Binding and Fidelity Determinants” details the 2.4 Angstrom resolution X-ray crystal structure of DNA polymerase IIIC (PolC) from Geobacillus kaustophilus.
These findings reveal a snap-shot view of how the nucleotide substrate interacts with the enzyme’s active site while it is bound to DNA template. This detailed understanding of the G. kaustophilus PolC structure should aid drug design of new antibiotics that target the closely related PolC enzymes from pathogenic organisms such as Staphylococcus aureus and Streptococcus pyogenes. The structure is a first of its kind and gives the highest resolution detail of any type-III polymerase ternary complex structure solved to date.
The PolC project was conducted as a collaboration with Replidyne, Inc. who utilized the contract research services of deCODE biostructures to provide three dimensional structures to support anti-infective development.
“We are fortunate to have the opportunity to collaborate on difficult problems and generate X-ray crystal structures which provide a unique understanding of a fundamental biological process and aid in developing new antibiotics” said Alex Burgin, COO at deCODE biostructures.
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