6q1m | pdb_00006q1m

Crystal structure of the wheat dwarf virus Rep domain

spinqualitylabelsall models 6q1m, resolution 1.24Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6q1m is a 1 chain structure with sequence from Wheat dwarf virus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.24Å Ligands: GOL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function REP_WDVS Essential for the replication of viral ssDNA. The closed circular ssDNA genome is first converted to a superhelical dsDNA. Rep binds a specific region at the genome origin of replication. It introduces an endonucleolytic nick within the conserved sequence 5'-TAATATTAC-3' in the intergenic region of the genome present in all geminiviruses, thereby initiating the rolling circle replication (RCR). Following cleavage, binds covalently to the 5'-phosphate of DNA as a tyrosyl ester. The cleavage gives rise to a free 3'-OH that serves as a primer for the cellular DNA polymerase. The polymerase synthesizes the (+) strand DNA by rolling circle mechanism. After one round of replication, a Rep-catalyzed nucleotidyl transfer reaction releases a circular single-stranded virus genome, thereby terminating the replication. Displays origin-specific DNA cleavage, nucleotidyl transferase, ATPase and helicase activities. Acts as an inhibitor of C-sense gene transcription (By similarity). 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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