5ZHZ
Crystal structure of the apurinic/apyrimidinic endonuclease IV from Mycobacterium tuberculosis
Summary for 5ZHZ
| Entry DOI | 10.2210/pdb5zhz/pdb |
| Descriptor | Probable endonuclease 4, SULFATE ION, ZINC ION, ... (4 entities in total) |
| Functional Keywords | endonuclease iv, tim fold, dna repair, apurinic-apyrimidinic (ap)ndonuclease superfamily, dna binding protein |
| Biological source | Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) |
| Total number of polymer chains | 1 |
| Total formula weight | 28193.50 |
| Authors | |
| Primary citation | Zhang, W.,Xu, Y.,Yan, M.,Li, S.,Wang, H.,Yang, H.,Zhou, W.,Rao, Z. Crystal structure of the apurinic/apyrimidinic endonuclease IV from Mycobacterium tuberculosis. Biochem. Biophys. Res. Commun., 498:111-118, 2018 Cited by PubMed 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 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 1.18 Å. 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. PubMed: 29496453DOI: 10.1016/j.bbrc.2018.02.181 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.18 Å) |
Structure validation
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