   5.1.3.31 | More |
the asymmetric unit contained two homologous subunits, and the dimer is generated by twofold symmetry. In MJ1311p, Glu125, Leu126 and Trp127 from one subunit are located over the metal-ion-binding site of the other subunit and contribute to the active site, narrowing the substrate-binding cleft. Three-dimensional structural analysis of MJ1311p, overview. The enzyme MJ1311p monomer is folded into an (alpha/beta)8 barrel carrying four additional helical segments, alpha1', alpha2', alpha4', and alpha6', which are inserted before alpha1, alpha2, alpha4, and alpha6, respectively. The quaternary-structural arrangement of MJ1311p is notably different from those of D-TE family enzymes |
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