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Atomic Structure of Thymidylate Synthase: Target for Rational Drug Design
Larry W. Hardy, Janet S. Finer-Moore, William R. Montfort, Melvin O. Jones, Daniel V. Santi and Robert M. Stroud
New Series, Vol. 235, No. 4787 (Jan. 23, 1987), pp. 448-455
Published by: American Association for the Advancement of Science
Stable URL: http://www.jstor.org/stable/1698341
Page Count: 8
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The atomic structure of thymidylate synthase from Lactobacillus casei was determined at 3 angstrom resolution. The native enzyme is a dimer of identical subunits. The dimer interface is formed by an unusual association between five-stranded $\beta $ sheets present in each monomer. Comparison of known sequences with the Lactobacillus casei structure suggests that they all have a common core structure around which loops are inserted or deleted in different sequences. Residues from both subunits contribute to each active site. Two arginine side chains can contribute to binding phosphate on the substrate. The side chains of several conserved amino acids can account for other determinants of substrate binding.
Science © 1987 American Association for the Advancement of Science