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Solution structure of TbTFIIS2‐1 PWWP domain from Trypanosoma brucei
Author(s) -
Wang Rui,
Zhang Jiahai,
Liao Shanhui,
Tu Xiaoming
Publication year - 2016
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.25035
Subject(s) - transcription (linguistics) , domain (mathematical analysis) , c terminus , dna , transcription factor , protein structure , chemistry , biology , genetics , microbiology and biotechnology , gene , biochemistry , amino acid , mathematical analysis , philosophy , linguistics , mathematics
TbTFIIS2‐1, one of the two TFIIS homologues of Trypanosome brucei ( T. brucei ), cooperates with TbTFIIS1 in regulating transcription in T. brcuei . Structurally divergent from other TFIIS homologues from higher organisms, TbTFIIS2‐1 contains an additional N‐terminal PWWP domain besides other three conserved domains, which may imply potential role of TbTFIIS2‐1 in transcription regulation. Here, we determined the solution structure of PWWP domain of TbTFIIS2‐1 by NMR spectroscopy, which was the first solution structure of PWWP domain solved in trypanosomatid. In spite of poor sequence similarity between PWWP domains, this domain of TbTFIIS2‐1 adopts a conserved 3D‐structure, which contains a five‐stranded β‐barrel and a C‐terminal α‐helix. Furthermore, we found that TbTFIIS2‐1 PWWP domain may be a protein–protein interaction module without the ability of DNA recognition and methyl‐group interaction. Proteins 2016; 84:912–919. © 2016 Wiley Periodicals, Inc.