A new insight into the zinc-dependent DNA-cleavage by the colicin E7 nuclease: a crystallographic and computational study

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F14%3A00437486" target="_blank" >RIV/61388963:_____/14:00437486 - isvavai.cz</a>
Result on the web
<a href="http://dx.doi.org/10.1039/c4mt00195h" target="_blank" >http://dx.doi.org/10.1039/c4mt00195h</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1039/c4mt00195h" target="_blank" >10.1039/c4mt00195h</a>

Result language
angličtina
Original language name
A new insight into the zinc-dependent DNA-cleavage by the colicin E7 nuclease: a crystallographic and computational study
Original language description
The nuclease domain of colicin E7 metallonuclease (NColE7) contains its active centre at the C-terminus. The mutant Delta N4-NColE7-C* - where the four N-terminal residues including the positively charged K446, R447 and K449 are replaced with eight residues from the GST tag - is catalytically inactive. The crystal structure of this mutant demonstrates that its overall fold is very similar to that of the native NColE7 structure. This implicates the stabilizing effect of the remaining N-terminal sequenceon the structure of the C-terminal catalytic site and the essential role of the deleted residues in the mechanism of the catalyzed reaction. Complementary QM/MM calculations on the protein-DNA complexes support the less favourable cleavage by the mutantprotein than by NColE7. Furthermore, a water molecule as a possible ligand for the Zn2+-ion is proposed to play a role in the catalytic process. These results suggest that the mechanism of the Zn2+-containing HNH nucleases needs to be fur
Czech name
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Czech description
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Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CF - Physical chemistry and theoretical chemistry
OECD FORD branch
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Project
<a href="/en/project/GA14-31419S" target="_blank" >GA14-31419S: Computational Design of Minimalistic Metallopeptides: ‘En Route’ to Disentangling the Catalytic Power of Metalloproteins</a><br>
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year
2014
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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