Structural highlights
Publication Abstract from PubMed
The Rep domain of Wheat dwarf virus (WDV Rep) is an HUH endonuclease involved in rolling-circle replication. HUH endonucleases coordinate a metal ion to enable the nicking of a specific ssDNA sequence and the subsequent formation of an intermediate phosphotyrosine bond. This covalent protein-ssDNA adduct makes HUH endonucleases attractive fusion tags (HUH-tags) in a diverse number of biotechnological applications. Solving the structure of an HUH endonuclease in complex with ssDNA will provide critical information about ssDNA recognition and sequence specificity, thus enabling rationally engineered protein-DNA interactions that are programmable. The structure of the WDV Rep domain reported here was solved in the apo state from a crystal diffracting to 1.24 A resolution and represents an initial step in the direction of solving the structure of a protein-ssDNA complex.
Crystal structure of the Wheat dwarf virus Rep domain.,Everett BA, Litzau LA, Tompkins K, Shi K, Nelson A, Aihara H, Evans Iii RL, Gordon WR Acta Crystallogr F Struct Biol Commun. 2019 Dec 1;75(Pt 12):744-749. doi:, 10.1107/S2053230X19015796. Epub 2019 Nov 27. PMID:31797816[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Everett BA, Litzau LA, Tompkins K, Shi K, Nelson A, Aihara H, Evans Iii RL, Gordon WR. Crystal structure of the Wheat dwarf virus Rep domain. Acta Crystallogr F Struct Biol Commun. 2019 Dec 1;75(Pt 12):744-749. doi:, 10.1107/S2053230X19015796. Epub 2019 Nov 27. PMID:31797816 doi:http://dx.doi.org/10.1107/S2053230X19015796