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. Author manuscript; available in PMC: 2008 Dec 4.

Published in final edited form as: Biotechnol Prog. 2007 Feb 22;23(2):364–369. doi: 10.1021/bp060287p

a) Model of P. furiosus β-glucosidase tetramer based on 3.3Å X-ray diffraction data (S.J.J. Brouns, T. Kaper, W.M. de Vos and J. van der Oost, unpublished data, used with permission). Subunits are depicted in Cα trace presentation. The single cysteine residue in each monomer is highlighted in ball and stick presentation. Distance between cysteine residues in intramolecular subunits is 67 Å or 38 Å, as illustrated, too far apart to contain a disulfide in the folded structure. b) Native PAGE shows similar predominantly tetrameric structure between wild-type (Lane 1) and C75S (Lane 2) β-glucosidase.

a) Model of P. furiosus β-glucosidase tetramer based on 3.3Å X-ray diffraction data (S.J.J. Brouns, T. Kaper, W.M. de Vos and J. van der Oost, unpublished data, used with permission). Subunits are depicted in Cα trace presentation. The single cysteine residue in each monomer is highlighted in ball and stick presentation. Distance between cysteine residues in intramolecular subunits is 67 Å or 38 Å, as illustrated, too far apart to contain a disulfide in the folded structure. b) Native PAGE shows similar predominantly tetrameric structure between wild-type (Lane 1) and C75S (Lane 2) β-glucosidase.