2M1H
Solution structure of a PWWP domain from Trypanosoma brucei
Summary for 2M1H
Entry DOI | 10.2210/pdb2m1h/pdb |
NMR Information | BMRB: 18474 |
Descriptor | Transcription elongation factor S-II (1 entity in total) |
Functional Keywords | transcription factor, transcription |
Biological source | Trypanosoma brucei |
Total number of polymer chains | 1 |
Total formula weight | 13247.49 |
Authors | |
Primary citation | Wang, R.,Zhang, J.,Liao, S.,Tu, X. Solution structure of TbTFIIS2-1 PWWP domain from Trypanosoma brucei. Proteins, 84:912-919, 2016 Cited by PubMed Abstract: 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. PubMed: 27005948DOI: 10.1002/prot.25035 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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