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

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Structure of the AvrBs3-DNA complex provides new insights into the initial thymine-recognition mechanism. / Stella, Stefano; Molina, Rafael; Yefimenko, Igor; Prieto, Jesús; Silva, George; Bertonati, Claudia; Juillerat, Alexandre; Duchateau, Phillippe; Montoya, Guillermo.

In: Acta Crystallographica Section D: Biological Crystallography, Vol. 69, No. 9, 2013, p. 1707-1716.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Stella, S, Molina, R, Yefimenko, I, Prieto, J, Silva, G, Bertonati, C, Juillerat, A, Duchateau, P & Montoya, G 2013, 'Structure of the AvrBs3-DNA complex provides new insights into the initial thymine-recognition mechanism', Acta Crystallographica Section D: Biological Crystallography, vol. 69, no. 9, pp. 1707-1716. https://doi.org/10.1107/S0907444913016429

APA

Stella, S., Molina, R., Yefimenko, I., Prieto, J., Silva, G., Bertonati, C., Juillerat, A., Duchateau, P., & Montoya, G. (2013). Structure of the AvrBs3-DNA complex provides new insights into the initial thymine-recognition mechanism. Acta Crystallographica Section D: Biological Crystallography, 69(9), 1707-1716. https://doi.org/10.1107/S0907444913016429

Vancouver

Stella S, Molina R, Yefimenko I, Prieto J, Silva G, Bertonati C et al. Structure of the AvrBs3-DNA complex provides new insights into the initial thymine-recognition mechanism. Acta Crystallographica Section D: Biological Crystallography. 2013;69(9):1707-1716. https://doi.org/10.1107/S0907444913016429

Author

Stella, Stefano ; Molina, Rafael ; Yefimenko, Igor ; Prieto, Jesús ; Silva, George ; Bertonati, Claudia ; Juillerat, Alexandre ; Duchateau, Phillippe ; Montoya, Guillermo. / Structure of the AvrBs3-DNA complex provides new insights into the initial thymine-recognition mechanism. In: Acta Crystallographica Section D: Biological Crystallography. 2013 ; Vol. 69, No. 9. pp. 1707-1716.

Bibtex

@article{a93ccf515a5e4dc581610ffb8176efaa,
title = "Structure of the AvrBs3-DNA complex provides new insights into the initial thymine-recognition mechanism",
abstract = "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 82kDa) 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.",
keywords = "gene targeting, genetics, protein-DNA interaction",
author = "Stefano Stella and Rafael Molina and Igor Yefimenko and Jes{\'u}s Prieto and George Silva and Claudia Bertonati and Alexandre Juillerat and Phillippe Duchateau and Guillermo Montoya",
year = "2013",
doi = "10.1107/S0907444913016429",
language = "English",
volume = "69",
pages = "1707--1716",
journal = "Acta Crystallographica Section D: Structural Biology",
issn = "2059-7983",
publisher = "International Union of Crystallography",
number = "9",

}

RIS

TY - JOUR

T1 - Structure of the AvrBs3-DNA complex provides new insights into the initial thymine-recognition mechanism

AU - Stella, Stefano

AU - Molina, Rafael

AU - Yefimenko, Igor

AU - Prieto, Jesús

AU - Silva, George

AU - Bertonati, Claudia

AU - Juillerat, Alexandre

AU - Duchateau, Phillippe

AU - Montoya, Guillermo

PY - 2013

Y1 - 2013

N2 - 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 82kDa) 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.

AB - 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 82kDa) 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.

KW - gene targeting

KW - genetics

KW - protein-DNA interaction

U2 - 10.1107/S0907444913016429

DO - 10.1107/S0907444913016429

M3 - Journal article

C2 - 23999294

AN - SCOPUS:84883588736

VL - 69

SP - 1707

EP - 1716

JO - Acta Crystallographica Section D: Structural Biology

JF - Acta Crystallographica Section D: Structural Biology

SN - 2059-7983

IS - 9

ER -

ID: 202332854