Article citationsMore>>
Oberpichler, I., Pierik, A., Wesslowski, J., Pokorny, R., Rosen, R., Vugman, M., Zhang, F., Neubauer, O., Ron, E., Batschauer, A. and Lamparter, T. (2011) A photolyase-like protein from Agrobacterium tumefaciens with an iron-sulfur cluster. PLoS ONE, 6, e26775.
doi:10.1371/journal.pone.0026775
has been cited by the following article:
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TITLE:
Molecular dynamics simulations of a DNA photolyase protein: High-mobility and conformational changes of the FAD molecule at low temperatures
AUTHORS:
Kholmirzo Kholmurodov, Ermuhammad Dushanov, Kenji Yasuoka
KEYWORDS:
Molecular Dynamics Simulations; DNA Photolyase; Conformation Change; FAD; MTHF; DNA
JOURNAL NAME:
Advances in Bioscience and Biotechnology,
Vol.3 No.3,
June
19,
2012
ABSTRACT: A molecular dynamics (MD) simulation is performed on a DNA photolyase to study the conformational behavior of the photoactive cofactor flavin adenine dinucleotide (FAD) inside the enzyme pocket. A DNA photolyase is a highly efficient light-driven enzyme that repairs the UV-induced cyclobutane pyrimidine dimer in damaged DNA. In this work, the FAD conformational and dynamic changes were studied within the total complex structure of a DNA photolyase protein (containing FADH–, MTHF, and DNA molecules) embedded in a water solvent. We aimed to compare the conformational changes of the FAD cofactor and other constituent fragments of the molecular system under consideration. The obtained results were discussed to gain insight into the light-driven mechanism of DNA repair by a DNA photolyase enzyme—based on the enzyme structure, the FAD mobility, and conformation shape.
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