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- Title
Multiple crystal forms of N, N′-diacetylchitobiose deacetylase from Pyrococcus furiosus.
- Authors
Nakamura, Tsutomu; Niiyama, Mayumi; Hashimoto, Wakana; Ida, Kurumi; Abe, Manabu; Morita, Junji; Uegaki, Koichi
- 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.
- Subjects
DEACETYLASES; PYROCOCCUS furiosus; SELENOMETHIONINE; CHEMICAL derivatives; N-terminal residues
- Publication
Acta Crystallographica: Section F, Structural Biology Communications, 2015, Vol 71, Issue 6, p657
- ISSN
2053-230X
- Publication type
Article
- DOI
10.1107/S2053230X15005695