Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
8293713 | Biochemical and Biophysical Research Communications | 2018 | 29 Pages |
Abstract
Endonuclease IV is a typical endonuclease of the apurinic-apyrimidinic (AP) or abasic endonuclease superfamily. It repairs damaged DNA through base excision repair by cleaving the DNA backbone immediately 5â² of an AP site. In Mycobacterium tuberculosis, endonuclease IV is the major AP endonuclease. This enzyme is absent from mammalian cells, making it an attractive target for anti-tuberculosis drug development. In this study, the structure of the recombinant endonuclease IV from M. tuberculosis (MtbEndo IV) was determined at a high resolution of 1.18â¯Ã
. MtbEndo IV was found to have a classical α8β8-fold TIM barrel with loops on its surface connecting the α-helices and β-strands that constitute a groove for DNA binding. Three zinc ions were identified at the active site. A comparison between the structures of MtbEndo IV and Escherichia coli End IV suggested that Gln32 of MtbEndo IV may plays a role in regulating substrate binding.
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Authors
Wei Zhang, Yueyang Xu, Mengrong Yan, Shanshan Li, Huiying Wang, Haitao Yang, Weihong Zhou, Zihe Rao,