Structure and dynamics of mesophilic variants from the homing endonuclease I-DmoI

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

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Structure and dynamics of mesophilic variants from the homing endonuclease I-DmoI. / Alba, Josephine; Marcaida, Maria Jose; Prieto, Jesus; Montoya, Guillermo; Molina, Rafael; D'Abramo, Marco.

In: Journal of Computer - Aided Molecular Design, Vol. 31, No. 12, 12.2017, p. 1063-1072.

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

Harvard

Alba, J, Marcaida, MJ, Prieto, J, Montoya, G, Molina, R & D'Abramo, M 2017, 'Structure and dynamics of mesophilic variants from the homing endonuclease I-DmoI', Journal of Computer - Aided Molecular Design, vol. 31, no. 12, pp. 1063-1072. https://doi.org/10.1007/s10822-017-0087-5

APA

Alba, J., Marcaida, M. J., Prieto, J., Montoya, G., Molina, R., & D'Abramo, M. (2017). Structure and dynamics of mesophilic variants from the homing endonuclease I-DmoI. Journal of Computer - Aided Molecular Design, 31(12), 1063-1072. https://doi.org/10.1007/s10822-017-0087-5

Vancouver

Alba J, Marcaida MJ, Prieto J, Montoya G, Molina R, D'Abramo M. Structure and dynamics of mesophilic variants from the homing endonuclease I-DmoI. Journal of Computer - Aided Molecular Design. 2017 Dec;31(12):1063-1072. https://doi.org/10.1007/s10822-017-0087-5

Author

Alba, Josephine ; Marcaida, Maria Jose ; Prieto, Jesus ; Montoya, Guillermo ; Molina, Rafael ; D'Abramo, Marco. / Structure and dynamics of mesophilic variants from the homing endonuclease I-DmoI. In: Journal of Computer - Aided Molecular Design. 2017 ; Vol. 31, No. 12. pp. 1063-1072.

Bibtex

@article{752a0b7f61004b6985218e71147ce11d,
title = "Structure and dynamics of mesophilic variants from the homing endonuclease I-DmoI",
abstract = "I-DmoI, from the hyperthermophilic archaeon Desulfurococcus mobilis, belongs to the LAGLIDADG homing endonuclease protein family. Its members are highly specific enzymes capable of recognizing long DNA target sequences, thus providing potential tools for genome manipulation. Working towards this particular application, many efforts have been made to generate mesophilic variants of I-DmoI that function at lower temperatures than the wild-type. Here, we report a structural and computational analysis of two I-DmoI mesophilic mutants. Despite very limited structural variations between the crystal structures of these variants and the wild-type, a different dynamical behaviour near the cleavage sites is observed. In particular, both the dynamics of the water molecules and the protein perturbation effect on the cleavage site correlate well with the changes observed in the experimental enzymatic activity.",
keywords = "Journal Article",
author = "Josephine Alba and Marcaida, {Maria Jose} and Jesus Prieto and Guillermo Montoya and Rafael Molina and Marco D'Abramo",
year = "2017",
month = dec,
doi = "10.1007/s10822-017-0087-5",
language = "English",
volume = "31",
pages = "1063--1072",
journal = "Journal of Computer-Aided Molecular Design",
issn = "0920-654X",
publisher = "Springer",
number = "12",

}

RIS

TY - JOUR

T1 - Structure and dynamics of mesophilic variants from the homing endonuclease I-DmoI

AU - Alba, Josephine

AU - Marcaida, Maria Jose

AU - Prieto, Jesus

AU - Montoya, Guillermo

AU - Molina, Rafael

AU - D'Abramo, Marco

PY - 2017/12

Y1 - 2017/12

N2 - I-DmoI, from the hyperthermophilic archaeon Desulfurococcus mobilis, belongs to the LAGLIDADG homing endonuclease protein family. Its members are highly specific enzymes capable of recognizing long DNA target sequences, thus providing potential tools for genome manipulation. Working towards this particular application, many efforts have been made to generate mesophilic variants of I-DmoI that function at lower temperatures than the wild-type. Here, we report a structural and computational analysis of two I-DmoI mesophilic mutants. Despite very limited structural variations between the crystal structures of these variants and the wild-type, a different dynamical behaviour near the cleavage sites is observed. In particular, both the dynamics of the water molecules and the protein perturbation effect on the cleavage site correlate well with the changes observed in the experimental enzymatic activity.

AB - I-DmoI, from the hyperthermophilic archaeon Desulfurococcus mobilis, belongs to the LAGLIDADG homing endonuclease protein family. Its members are highly specific enzymes capable of recognizing long DNA target sequences, thus providing potential tools for genome manipulation. Working towards this particular application, many efforts have been made to generate mesophilic variants of I-DmoI that function at lower temperatures than the wild-type. Here, we report a structural and computational analysis of two I-DmoI mesophilic mutants. Despite very limited structural variations between the crystal structures of these variants and the wild-type, a different dynamical behaviour near the cleavage sites is observed. In particular, both the dynamics of the water molecules and the protein perturbation effect on the cleavage site correlate well with the changes observed in the experimental enzymatic activity.

KW - Journal Article

U2 - 10.1007/s10822-017-0087-5

DO - 10.1007/s10822-017-0087-5

M3 - Journal article

C2 - 29177929

VL - 31

SP - 1063

EP - 1072

JO - Journal of Computer-Aided Molecular Design

JF - Journal of Computer-Aided Molecular Design

SN - 0920-654X

IS - 12

ER -

ID: 186153053