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We report the crystal structure of PYCH_01220, a hypothetical protein in Pyrococcus yayanosii CH1. This protein is composed of two domains, named Domain A and Domain B. While Domain B is not significantly homologous to known protein structures, Domain A is structurally analogous to the C-terminal ribonuclease domain of Escherichia coli colicin D. Domain A has a positively charged surface patch rendered by 13 basic residues, eight arginine or lysine residues of which are evolutionarily conserved. Electrophoretic mobility shift assays showed that PYCH_01220 binds to DNA, and charge-inversion mutations on this patch negatively affect the DNA binding, suggesting that the function of PYCH_01220 might involve nucleic acid-binding via the positively charged patch. © 2020 Wiley Periodicals LLC.


Haemin Noh, Jae-Hyun Jeon, Yeon-Gil Kim, Byung-Ha Oh. Crystal structure of PYCH_01220 from Pyrococcus yayanosii potentially involved in binding nucleic acid. Proteins. 2021 Apr;89(4):468-472

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PMID: 33236809

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