4xm0

N,N'-diacetylchitobiose deacetylase (SeMet derivative) from Pyrococcus furiosus in the absence of cadmium

spinqualitylabelsall models 4xm0, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4xm0 is a 6 chain structure with sequence from Pyrococcus furiosus DSM 3638. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.8Å Ligands: MSE, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q8U3V1_PYRFU Publication Abstract from PubMed 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. Multiple crystal forms of N,N'-diacetylchitobiose deacetylase from Pyrococcus furiosus.,Nakamura T, Niiyama M, Hashimoto W, Ida K, Abe M, Morita J, Uegaki K Acta Crystallogr F Struct Biol Commun. 2015 Jun;71(Pt 6):657-62. doi:, 10.1107/S2053230X15005695. Epub 2015 May 20. PMID:26057790 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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