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Publication Abstract from PubMed

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 5' 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 1.18A. MtbEndo IV was found to have a classical alpha8beta8-fold TIM barrel with loops on its surface connecting the alpha-helices and beta-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.

Crystal structure of the apurinic/apyrimidinic endonuclease IV from Mycobacterium tuberculosis.,Zhang W, Xu Y, Yan M, Li S, Wang H, Yang H, Zhou W, Rao Z Biochem Biophys Res Commun. 2018 Mar 25;498(1):111-118. doi:, 10.1016/j.bbrc.2018.02.181. Epub 2018 Feb 27. PMID:29496453^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.