6iml
The crystal structure of AsfvLIG:CT1 complex
Structural highlights
FunctionDNLI_ASFB7 Very low-fidelity DNA ligase that seals nicks in double-stranded DNA during DNA repair (PubMed:15938630). Together with the viral repair DNA polymerase X, fills the single nucleotide gaps generated by the AP endonuclease (PubMed:15938630). It is not essential for viral replication and recombination (PubMed:15938630). Displays a very low adenylation activity towards DNA with 3'-dideoxy- or 3'-amino-terminated nicks compared to regular nick DNA (PubMed:15938630).[1] Publication Abstract from PubMedAfrican swine fever virus (ASFV) is contagious and can cause highly lethal disease in pigs. ASFV DNA ligase (AsfvLIG) is one of the most error-prone ligases identified to date; it catalyzes DNA joining reaction during DNA repair process of ASFV and plays important roles in mutagenesis of the viral genome. Here, we report four AsfvLIG:DNA complex structures and demonstrate that AsfvLIG has a unique N-terminal domain (NTD) that plays critical roles in substrate binding and catalytic complex assembly. In combination with mutagenesis, in vitro binding and catalytic assays, our study reveals that four unique active site residues (Asn153 and Leu211 of the AD domain; Leu402 and Gln403 of the OB domain) are crucial for the catalytic efficiency of AsfvLIG. These unique structural features can serve as potential targets for small molecule design, which could impair genome repair in ASFV and help combat this virus in the future. Structure of the error-prone DNA ligase of African swine fever virus identifies critical active site residues.,Chen Y, Liu H, Yang C, Gao Y, Yu X, Chen X, Cui R, Zheng L, Li S, Li X, Ma J, Huang Z, Li J, Gan J Nat Commun. 2019 Jan 23;10(1):387. doi: 10.1038/s41467-019-08296-w. PMID:30674878[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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