PMID:3072020

Citation	Seville, M, Vincent, MG and Hahn, K (1988) Modeling the three-dimensional structures of bacterial aminotransferases. Biochemistry 27:8344-9
Abstract	The refined crystallographic structure of the "closed" conformation of chicken mitochondrial aspartate aminotransferase has been used as a template for the construction of models of the two Escherichia coli aminotransferases encoded by the tyrB and aspC genes. The main results are as follows: (1) Only minor changes are required in the coordinates of the backbone atoms to accommodate the large number of substituted side chains. (2) All deletions and insertions required to allow maximum primary sequence alignment are on the solvent-accessible surface. (3) Charged residues are all located on the surface, in contact with solvent, except for certain conserved active site residues. (4) The close packing within the hydrophobic core is maintained. (5) The interactions between the subunits are maintained. (6) Modeling of tyrosine as an external aldimine into the active sites points to several residues that could be involved in determining the substrate specificities of these aminotransferases.
Links	PubMed
Keywords	Binding Sites; Escherichia coli/enzymology; Models, Molecular; Molecular Structure; Protein Conformation; Substrate Specificity; Transaminases/metabolism
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Significance

Gene product	Qualifier	GO Term	Evidence Code	with/from	Aspect	Extension	Notes	Status
ECOLI:TYRB		GO:0070547: L-tyrosine aminotransferase activity	ECO:0000315:		F		"The refined crystallographic structure of the "closed" conformation of chicken mitochondrial aspartate aminotransferase has been used as a template for the construction of models of the two Escherichia coli aminotransferases encoded by the tyrB and aspC genes"	complete CACAO 4694

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