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2M1H

Solution structure of a PWWP domain from Trypanosoma brucei

Summary for 2M1H
Entry DOI10.2210/pdb2m1h/pdb
NMR InformationBMRB: 18474
DescriptorTranscription elongation factor S-II (1 entity in total)
Functional Keywordstranscription factor, transcription
Biological sourceTrypanosoma brucei
Total number of polymer chains1
Total formula weight13247.49
Authors
Wang, R.,Fan, K.,Liao, S.,Zhang, J.,Tu, X. (deposition date: 2012-11-28, release date: 2013-12-04, Last modification date: 2024-05-15)
Primary citationWang, 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: 27005948
DOI: 10.1002/prot.25035
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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