Premium
Crystal structure of the wheat dwarf virus Rep domain
Author(s) -
Litzau Lauren Anne
Publication year - 2020
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.2020.34.s1.02954
Subject(s) - dna , endonuclease , computational biology , domain (mathematical analysis) , biology , chemistry , genetics , mathematical analysis , mathematics
The wheat dwarf virus Rep domain is an HUH‐endonuclease and is involved in rolling‐circle replication. HUH‐endonucleases, or HUH‐tags, form covalent protein‐ssDNA adducts by coordinating a divalent metal ion to cleave a specific ssDNA sequence and form a phosphotyrosine linkage. This protein‐ssDNA fusion is useful for various biotechnology applications such as cellular imaging, cellular barcoding, DNA‐guided protein localization, and single molecule manipulation of DNA‐tethered proteins. Solving the structure of the Rep domain in complex with DNA could present necessary information regarding HUH‐tag sequence specificity and allow for rational engineering of protein‐DNA interactions. Here, the structure of WDV Rep domain in the apo state was solved with a crystal diffracting to 1.24 Å. While ssDNA soaks were attempted, they proved ineffective. However, the solved structure represents a step towards solving protein‐ssDNA complex. Support or Funding Information 1. National Institutes of Health/National Institute of General Medical Sciences (grant No. GM119483); NIH (grant No.242 NIGMS R35‐GM118047)