1.1.99.28 | hanging drop method, crystal structure of oxidized preGFOR R30K/R31K, in complex with succinate (preGFOR(succ)) and with glycerol (PreGFOR(gll)), at 2.2 A and 2.05 A resolution, respectively, and of reduced preGFOR R30K/R31K, after incubation with glucose (preGFOR(Glu)) and with sorbitol (preGFOR(sorb)) at 2.5 A and 2.6 A resolution. In all four crystal structures, the signal peptide is disordered, implying a flexibility that may be important for its interaction with the translocation apparatus. The crystal structures show that the mature enzyme portion of preGFOR is identical to native GFOR, in structure and cofactor binding |