THE CRYSTAL-STRUCTURE OF HUMAN MUSCLE ALDOLASE AT 3.0 A-RESOLUTION

The three-dimensional structure of fructose-1,6-bisphosphate aldolase from human muscle has been determined at 3.0 Å resolution by X-ray crystallography. The active protein is a tetramer of 4 identical subunits each of which is composed of an eight-stranded α/β-barrel structure. The lysine residue responsible for Schiff base formation with the substrate is located near the centre of the barrel in the middle of the sixth β-strand. While the overall topology of the α/β-barrel is very similar to those found in several other enzymes, the distribution of charged residues inside the core of the barrel seems distinct. The quaternary fold of human muscle aldolase uses interfacial regions also involved in the subunit association of other α/β-barrel proteins found in glycolysis, but exploits these regions in a manner not seen previously. © 1990.