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3OSF

The structure of protozoan parasite Trichomonas vaginalis Myb2 in complex with MRE-2f-13 DNA

Summary for 3OSF
Entry DOI10.2210/pdb3osf/pdb
Related3OSG
DescriptorMYB21, 5'-D(*CP*TP*GP*TP*AP*TP*CP*GP*TP*CP*TP*TP*G)-3', 5'-D(*CP*AP*AP*GP*AP*CP*GP*AP*TP*AP*CP*AP*G)-3', ... (5 entities in total)
Functional Keywordstranscription-dna complex, myb2, r2r3 domain, dna binding protein, transcription factor, nucleus, transcription/dna
Biological sourceTrichomonas vaginalis
Total number of polymer chains6
Total formula weight45714.64
Authors
Jiang, I.,Tsai, C.K.,Chen, S.C.,Wang, S.H.,Amiraslanov, I.,Chang, C.F.,Wu, W.J.,Tai, J.H.,Liaw, Y.C.,Huang, T.H. (deposition date: 2010-09-09, release date: 2011-08-03, Last modification date: 2024-03-20)
Primary citationJiang, I.,Tsai, C.K.,Chen, S.C.,Wang, S.H.,Amiraslanov, I.,Chang, C.F.,Wu, W.J.,Tai, J.H.,Liaw, Y.C.,Huang, T.H.
Molecular basis of the recognition of the ap65-1 gene transcription promoter elements by a Myb protein from the protozoan parasite Trichomonas vaginalis.
Nucleic Acids Res., 39:8992-9008, 2011
Cited by
PubMed Abstract: Iron-inducible transcription of the ap65-1 gene in Trichomonas vaginalis involves at least three Myb-like transcriptional factors (tvMyb1, tvMyb2 and tvMyb3) that differentially bind to two closely spaced promoter sites, MRE-1/MRE-2r and MRE-2f. Here, we defined a fragment of tvMyb2 comprising residues 40-156 (tvMyb2₄₀₋₁₅₆) as the minimum structural unit that retains near full binding affinity with the promoter DNAs. Like c-Myb in vertebrates, the DNA-free tvMyb2₄₀₋₁₅₆ has a flexible and open conformation. Upon binding to the promoter DNA elements, tvMyb2₄₀₋₁₅₆ undergoes significant conformational re-arrangement and structure stabilization. Crystal structures of tvMyb2₄₀₋₁₅₆ in complex with promoter element-containing DNA oligomers showed that 5'-a/gACGAT-3' is the specific base sequence recognized by tvMyb2₄₀₋₁₅₆, which does not fully conform to that of the Myb binding site sequence. Furthermore, Lys⁴⁹, which is upstream of the R2 motif (amino acids 52-102) also participates in specific DNA sequence recognition. Intriguingly, tvMyb2₄₀₋₁₅₆ binds to the promoter elements in an orientation opposite to that proposed in the HADDOCK model of the tvMyb1₃₅₋₁₄₁/MRE-1-MRE-2r complex. These results shed new light on understanding the molecular mechanism of Myb-DNA recognition and provide a framework to study the molecular basis of transcriptional regulation of myriad Mybs in T. vaginalis.
PubMed: 21771861
DOI: 10.1093/nar/gkr558
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.032 Å)
Structure validation

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