3ZFK

N-terminal truncated Nuclease Domain of Colicin E7

3ZFK の概要

• エントリーDOI: 10.2210/pdb3zfk/pdb
• 分子名称: COLICIN-E7, ZINC ION, CHLORIDE ION, ... (6 entities in total)
• 機能のキーワード: hydrolase, artificial metallonuclease, allosteric control
• 由来する生物種: ESCHERICHIA COLI
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 31814.86

構造登録者

Toth, E.,Czene, A.,Gyurcsik, B.,Otten, H.,Poulsen, J.-C.N.,Larsen, S.,Christensen, H.E.M.,Nagata, K. (登録日: 2012-12-11, 公開日: 2013-12-18, 最終更新日: 2023-12-20)

主引用文献

Czene, A.,Toth, E.,Nemeth, E.,Otten, H.,Poulsen, J.N.,Christensen, H.E.M.,Rulisek, L.,Nagata, K.,Larsen, S.,Gyurcsik, B.
A New Insight Into the Zinc-Dependent DNA-Cleavage by the Colicin E7 Nuclease: A Crystallographic and Computational Study.
Metallomics, 6:2090-, 2014

PubMed Abstract: The nuclease domain of colicin E7 metallonuclease (NColE7) contains its active centre at the C-terminus. The mutant ΔN4-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 sequence on 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 mutant protein than by NColE7. Furthermore, a water molecule as a possible ligand for the Zn(2+)-ion is proposed to play a role in the catalytic process. These results suggest that the mechanism of the Zn(2+)-containing HNH nucleases needs to be further studied and discussed.

PubMed: 25179124
DOI: 10.1039/C4MT00195H

実験手法

X-RAY DIFFRACTION (1.7 Å)