|
|||||
|
|
Structure of the Ni(II) complex of Escherichia coli peptide deformylase and suggestions on deformylase activities depending on different metal(II) centres |
|
| Authors: | Ngo Thi Hai Yen Xenia Bogdanović Gottfried J. Palm Olaf Kühl Winfried Hinrichs |
| Affiliation: | (1) Department of Molecular Structural Biology, Institute for Biochemistry, University of Greifswald, Felix-Hausdorff-Str. 4, 17489 Greifswald, Germany;(2) Bioinorganic Research Group, Institute for Biochemistry, University of Greifswald, Felix-Hausdorff-Str. 4, 17489 Greifswald, Germany;(3) Present address: Institute of Industrial Chemistry, Center for Pharmaceutical Chemistry, N2 Pham Ngu Lao Street, Hoan Kiem District, Hanoi, Vietnam; |
| Abstract: | Crystal structures of polypeptide deformylase (PDF) of Escherichia coli with nickel(II) replacing the native iron(II) have been solved with chloride and formate as metal ligands. The chloro complex is a model for the correct protonation state of the hydrolytic hydroxo ligand and the protonated status of the Glu133 side chain as part of the hydrolytic mechanism. The ambiguity that recently some PDFs have been identified with Zn2+ ion as the active-site centre whereas others are only active with Fe2+ (or Co2+, Ni2+) is discussed with respect to Lewis acid criteria of the metal ion and substrate activation by the CD loop. |
| Keywords: | |
| 本文献已被 SpringerLink 等数据库收录！ | |