Tetragonal crystal structure of mung bean inhibitor porcine trypsin complex

Crystal structure of the mung bean inhibitor-porcine trypsin (1 : 2) ternary complex in the tetragonal crystal with space group I422 was determined at 0.25 nm resolution. 56 residues of the mung bean inhibitor were resolved among which one more residue Pro11 was determined than the previously reported structure in the trigonal crystal of the same complex. The structure of the inhibitor in the tetragonal crystal is similar to that in the trigonal crystal and the complexes in tetragonal crystal is also in packing disorder as in trigonal crystal, i. e., the complexes pack in two orientations Ta : MaMb i Tb and Tb : MbMa : Ta (Ta, Tb = trypsin, Ma, Mb = loop I and loop Il of mung bean inhibitor respectively). But there are some differences in the two crystal forms. First, the inhibitor in the tetragonal crystal has no pseudo-beta-sheet structure which the trigonal crystal has. Second, its conformation is somewhat different from that in the trigonal crystal. Analysis showed that the linkage peptides between the two rigid domains of the inhibitor were flexible, which also accounted for the formation of different crystal forms of this complex. Moreover, comparing mung bean inhibitor to other Bowman-Birk inhibitors showed that the two double-stranded antiparallel beta-sheets and the reactive binding loops were highly conservative.Biochemistry & Molecular BiologyBiophysicsSCI(E)PubMed0ARTICLE4357-3623