Determining the DUF55-domain structure of human thymocyte nuclear protein 1 from crystals partially twinned by tetartohedry.
Human thymocyte nuclear protein 1 contains a unique DUF55 domain consisting of 167 residues (55-221), but its cellular function remains unclear. Crystals of DUF55 belonged to the trigonal space group P3(1), but twinning caused the data to approach apparent 622 symmetry. Two data sets were collected to 2.3 A resolution. Statistical analysis confirmed that both data sets were partially twinned by tetartohedry. Tetartohedral twin fractions were estimated. After the structure had been determined, only one twofold axis of rotational pseudosymmetry was found in the crystal structure. Using the DALI program, a YTH domain, which is a potential RNA-binding domain from human YTH-domain-containing protein 2, was identified as having the most similar three-dimensional fold to that of DUF55. It is thus implied that DUF55 might be a potential RNA-related domain.
Yu
Feng
F
Shanghai Institute of Applied Physics, Chinese Academy of Sciences, People's Republic of China.
Song
Aixin
A
Xu
Chunyan
C
Sun
Lihua
L
Li
Jian
J
Tang
Lin
L
Yu
Minmin
M
Yeates
Todd O
TO
Hu
Hongyu
H
He
Jianhua
J
D001665:Binding Sites; D003460:Crystallization; D018360:Crystallography, X-Ray; D006801:Humans; D008958:Models, Molecular; D009419:Nerve Tissue Proteins / Q000737:chemistry; D009687:Nuclear Proteins / Q000737:chemistry*; D010446:Peptide Fragments / Q000737:chemistry; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D000072260:RNA Splicing Factors; D016601:RNA-Binding Proteins / Q000737:chemistry*
D009419:Nerve Tissue Proteins; D009687:Nuclear Proteins; D010446:Peptide Fragments; D000072260:RNA Splicing Factors; D016601:RNA-Binding Proteins; C505706:THYN1 protein, human; C490769:YTHDC1 protein, human