Hl. Carrell et al., MODES OF BINDING SUBSTRATES AND THEIR ANALOGS TO THE ENZYME D-XYLOSE ISOMERASE, Acta crystallographica. Section D, Biological crystallography, 50, 1994, pp. 113-123
Studies of binding of substrates and inhibitors of the enzyme D-xylose
isomerase show, from X-ray diffraction data at 1.6-1.9 angstrom resol
ution, that there are a variety of binding modes. These vary in the ma
nner in which the substrate or its analogue extend, on binding, across
the carboxy end of the (betaalpha)8-barrel structure. These binding s
ites are His54 and the metal ion (magnesium or manganese) that is held
in place by Glu18l, Asp245, Glu217 and Asp287. Possible catalytic gro
ups have been identified in proposed mechanisms and their role in the
binding of ligands is illustrated.