View source for 3zqc


==Structure of the Trichomonas vaginalis Myb3 DNA-binding domain bound to a promoter sequence reveals a unique C-terminal beta-hairpin conformation==
<StructureSection load='3zqc' size='340' side='right'caption='[[3zqc]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3zqc]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Trichomonas_vaginalis Trichomonas vaginalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZQC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZQC FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3zqc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zqc OCA], [https://pdbe.org/3zqc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zqc RCSB], [https://www.ebi.ac.uk/pdbsum/3zqc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zqc ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A2D9X4_TRIV3 A2D9X4_TRIV3] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Trichomonas vaginalis Myb3 transcription factor (tvMyb3) recognizes the MRE-1 promoter sequence and regulates ap65-1 gene, which encodes a hydrogenosomal malic enzyme that may play a role in the cytoadherence of the parasite. Here, we identified tvMyb3(53-180) as the essential fragment for DNA recognition and report the crystal structure of tvMyb3(53-180) bound to MRE-1 DNA. The N-terminal fragment adopts the classical conformation of an Myb DNA-binding domain, with the third helices of R2 and R3 motifs intercalating in the major groove of DNA. The C-terminal extension forms a beta-hairpin followed by a flexible tail, which is stabilized by several interactions with the R3 motif and is not observed in other Myb proteins. Interestingly, this unique C-terminal fragment does not stably connect with DNA in the complex structure but is involved in DNA binding, as demonstrated by NMR chemical shift perturbation, (1)H-(15)N heteronuclear-nuclear Overhauser effect and intermolecular paramagnetic relaxation enhancement. Site-directed mutagenesis also revealed that this C-terminal fragment is crucial for DNA binding, especially the residue Arg(153) and the fragment K(170)KRK(173). We provide a structural basis for MRE-1 DNA recognition and suggest a possible post-translational regulation of tvMyb3 protein.

Structure of the Trichomonas vaginalis Myb3 DNA-binding domain bound to a promoter sequence reveals a unique C-terminal beta-hairpin conformation.,Wei SY, Lou YC, Tsai JY, Ho MR, Chou CC, Rajasekaran M, Hsu HM, Tai JH, Hsiao CD, Chen C Nucleic Acids Res. 2012 Jan;40(1):449-60. Epub 2011 Sep 8. PMID:21908401<ref>PMID:21908401</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3zqc" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Trichomonas vaginalis]]
[[Category: Chen C]]
[[Category: Hsiao C-D]]
[[Category: Hsu H-M]]
[[Category: Lou Y-C]]
[[Category: Tai J-H]]
[[Category: Tsai J-Y]]
[[Category: Wei S-Y]]