A structural model for the glutamate-specific endopeptidase from Streptomyces griseus that explains substrate specificity.
We present a model for the three-dimensional structure of the glutamate-specific endopeptidase from Streptomyces griseus based on the crystal structures of other bacterial proteases of the trypsin family. For the first time a structural model is described which attempts to explain the basis of P1 glutamate specificity in serine proteases. Several important changes to the S1 pocket with respect to other members of the family of different specificity are described. Of particular interest is the presence of a histidine at position 213 and the substitution of Arg-138 by lysine. Other biochemical evidence concerning substrate preferences can be rationalized on the basis of the model.
Instituto de Física e Química de São Carlos, Departamento de Física e Ciência dos Materiais, Universidade de São Paulo, Brasil.
J A
JA
Barbosa
R C
RC
Garratt
J W
JW
Saldanha
D000595:Amino Acid Sequence; D003196:Computer Graphics; D008961:Models, Structural; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D017386:Sequence Homology, Amino Acid; D012697:Serine Endopeptidases / Q000737:chemistry* / Q000378:metabolism*; D013305:Streptomyces griseus / Q000201:enzymology*; D013379:Substrate Specificity; D014357:Trypsin / Q000737:chemistry
D012697:Serine Endopeptidases; D014357:Trypsin; C069136:glutamyl endopeptidase II