PDBsum entry 2m1h

Transcription

PDB id: 2m1h

Contents

Protein chain

110 a.a.

PDB id:

2m1h

Name:

Transcription

Title:

Solution structure of a pwwp domain from trypanosoma brucei

Structure:

Transcription elongation factor s-ii. Chain: a. Fragment: pwwp domain (unp residues 1-110). Engineered: yes

Source:

Trypanosoma brucei. Organism_taxid: 5691. Gene: tb927.2.3580. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

20 models

Authors:

R.Wang,K.Fan,S.Liao,J.Zhang,X.Tu

Key ref:

R.Wang et al. (2016). Solution structure of TbTFIIS2-1 PWWP domain from Trypanosoma brucei. Proteins, 84, 912-919. PubMed id: 27005948 DOI: 10.1002/prot.25035

Date:

28-Nov-12 Release date: 04-Dec-13

Protein chain

Q586X9  (Q586X9_TRYB2) -  Transcription elongation factor S-II, putative from Trypanosoma brucei brucei (strain 927/4 GUTat10.1)

Seq: 467 a.a.

Struc: 110 a.a.

DOI no: 10.1002/prot.25035

Proteins 84:912-919 (2016)

PubMed id: 27005948

Solution structure of TbTFIIS2-1 PWWP domain from Trypanosoma brucei.

R.Wang, J.Zhang, S.Liao, X.Tu.

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.