View source for 2ypf


==Structure of the AvrBs3-DNA complex provides new insights into the initial thymine-recognition mechanism==
<StructureSection load='2ypf' size='340' side='right'caption='[[2ypf]], [[Resolution|resolution]] 2.55&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2ypf]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Xanthomonas_campestris Xanthomonas campestris] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YPF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YPF 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]] 2.55&#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=2ypf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ypf OCA], [https://pdbe.org/2ypf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ypf RCSB], [https://www.ebi.ac.uk/pdbsum/2ypf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ypf ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q3ZD73_XANCA Q3ZD73_XANCA] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Transcription activator-like effectors contain a DNA-binding domain organized in tandem repeats. The repeats include two adjacent residues known as the repeat variable di-residue, which recognize a single base pair, establishing a direct code between the dipeptides and the target DNA. This feature suggests this scaffold as an excellent candidate to generate new protein-DNA specificities for biotechnological applications. Here, the crystal structure of AvrBs3 (residues 152-895, molecular mass 82 kDa) in complex with its target DNA sequence is presented, revealing a new mode of interaction with the initial thymine of the target sequence, together with an analysis of both the binding specificity and the thermodynamic properties of AvrBs3. This study quantifies the affinity and the specificity between AvrBs3 and its target DNA. Moreover, in vitro and in vivo analyses reveal that AvrBs3 does not show a strict nucleotide-binding preference for the nucleotide at the zero position of the DNA, widening the number of possible sequences that could be targeted by this scaffold.

Structure of the AvrBs3-DNA complex provides new insights into the initial thymine-recognition mechanism.,Stella S, Molina R, Yefimenko I, Prieto J, Silva G, Bertonati C, Juillerat A, Duchateau P, Montoya G Acta Crystallogr D Biol Crystallogr. 2013 Sep 1;69(Pt 9):1707-16. doi:, 10.1107/S0907444913016429. Epub 2013 Aug 15. PMID:23999294<ref>PMID:23999294</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2ypf" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Synthetic construct]]
[[Category: Xanthomonas campestris]]
[[Category: Bertonati C]]
[[Category: Duchateau P]]
[[Category: Juillerat A]]
[[Category: Molina R]]
[[Category: Montoya G]]
[[Category: Prieto J]]
[[Category: Silva GH]]
[[Category: Stella S]]
[[Category: Yefimenko I]]