Premium
Crystal structure of PYCH_01220 from Pyrococcus yayanosii potentially involved in binding nucleic acid
Author(s) -
Noh Haemin,
Jeon JaeHyun,
Kim YeonGil,
Oh ByungHa
Publication year - 2021
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.26029
Subject(s) - nucleic acid , dna , chemistry , binding domain , escherichia coli , lysine , biochemistry , biology , crystallography , biophysics , binding site , amino acid , gene
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.