Crystal structure of the Wheat dwarf virus Rep domain Everett Blake A.

Blake A. Everett, Lauren A. Litzau, Kassidy Tompkins, Ke Shi, Andrew Nelson, Hideki Aihara, Robert L.Evans Evans, Wendy R. Gordon

Research output: Contribution to journalArticlepeer-review

Abstract

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 1.24Å resolution and represents an initial step in the direction of solving the structure of a protein-ssDNA complex.

Original languageEnglish (US)
Pages (from-to)744-749
Number of pages6
JournalActa Crystallographica Section F: Structural Biology Communications
Volume75
DOIs
StatePublished - Dec 1 2019

Bibliographical note

Funding Information:
Funding for this research was provided by: National Institutes of Health/National Institute of General Medical Sciences (grant No. GM119483); NIH (grant No. NIGMS R35-GM118047).

Publisher Copyright:
© 2019 International Union of Crystallography.

Keywords

  • HUH motif
  • HUH-tag
  • Rep domain
  • Wheat dwarf virus
  • crystal structure
  • engineered protein-ssDNA complexes National Institute of General Medical Sciences GM119483 NIGMS R35-GM118047
  • ssDNA

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