PH1010 Swiss:O58738 is composed of five alpha-helices (1-5) and eight beta-strands (1-8) with the following topology: beta-1, alpha-1, beta-2, beta-3, alpha-2, alpha-3, beta-4, beta-5, alpha-4, beta-6, alpha-5, beta-7, beta-8. The first six beta-strands (1-6) form a slightly twisted antiparallel beta-sheet and face five alpha-helices on one side. The last two beta-strands form an antiparallel beta-sheet in the C-terminus. PH1010 forms a characteristic homodimer structure in the crystal. Dimerisation of the molecule is crucial for function. The structure resembles that of some ribosomal proteins such as the 50S ribosomal protein L5 [1]. Although the structure resembles that of the RRM-type RNA-binding domain of the ribosomal L5 protein, the residues involved in RNA-binding in the L5 protein are not conserved in this family [2]. Despite this, these proteins bind to double-stranded RNA in a non-sequence specific manner [3]. [1]. 18831045. Crystal structure of the DUF54 family protein PH1010 from hyperthermophilic archaea Pyrococcus horikoshii OT3. Miyazono KI, Shirokane M, Sawano Y, Tanokura M;. Proteins. 2008;74:256-260. [2]. 19079550. UPF201 archaeal specific family members reveal structural similarity to RNA-binding proteins but low likelihood for RNA-binding function. Rao KN, Burley SK, Swaminathan S;. PLoS One. 2008;3:e3903. [3]. 20380716. Expression, purification and structural analysis of the Pyrococcus abyssi RNA binding protein PAB1135. Luz JS, Barbosa JA, Ramos CR, Oliveira CC;. BMC Res Notes. 2010;3:97. (from Pfam)
- Date:
- 2024-10-16