2ypf

Structure of the AvrBs3-DNA complex provides new insights into the initial thymine-recognition mechanism

spinqualitylabelsall models 2ypf, resolution 2.55Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2ypf is a 3 chain structure with sequence from Xanthomonas campestris and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.55Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q3ZD73_XANCA 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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