Download MendeleyMultiple crystal forms of N,N'-diacetylchitobiose deacetylase from Pyrococcus furiosus.
Nakamura, T., Niiyama, M., Hashimoto, W., Ida, K., Abe, M., Morita, J., Uegaki, K.(2015) Acta Crystallogr F Struct Biol Commun 71: 657-662
- PubMed: 26057790
- DOI: https://doi.org/10.1107/S2053230X15005695
- Primary Citation of Related Structures:
4XLZ, 4XM0, 4XM1, 4XM2 - PubMed Abstract:
Native N,N'-diacetylchitobiose deacetylase from Pyrococcus furiosus (Pf-Dac) and its selenomethionine derivative (Se-Pf-Dac) were crystallized and analyzed in the presence and absence of cadmium ion. The four crystal structures fell into three different crystal-packing groups, with the cadmium-free Pf-Dac and Se-Pf-Dac belonging to the same space group, with homologous unit-cell parameters. The crystal structures in the presence of cadmium contained distorted octahedral cadmium complexes coordinated by three chlorides, two O atoms and an S or Se atom from the N-terminal methionine or selenomethionine, respectively. The N-terminal cadmium complex was involved in crystal contacts between symmetry-related molecules through hydrogen bonding to the N-termini. While all six N-termini of Se-Pf-Dac were involved in cadmium-complex formation, only two of the Pf-Dac N-termini participated in complex formation in the Cd-containing crystal, resulting in different crystal forms. These differences are discussed in light of the higher stability of the Cd-Se bond than the Cd-S bond. This work provides an example of the contribution of cadmium towards determining protein crystal quality and packing depending on the use of the native protein or the selenomethionine derivative.
- National Institute of Advanced Industrial Science and Technology, Ikeda, Osaka 563-8577, Japan.
Organizational Affiliation:
