Structural highlights
Publication Abstract from PubMed
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. This article is protected by copyright. All rights reserved.
Crystal structure of PYCH_01220 from Pyrococcus yayanosii potentially involved in binding nucleic acid.,Noh H, Jeon JH, Kim YG, Oh BH Proteins. 2020 Nov 25. doi: 10.1002/prot.26029. PMID:33236809[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Noh H, Jeon JH, Kim YG, Oh BH. Crystal structure of PYCH_01220 from Pyrococcus yayanosii potentially involved in binding nucleic acid. Proteins. 2020 Nov 25. doi: 10.1002/prot.26029. PMID:33236809 doi:http://dx.doi.org/10.1002/prot.26029