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Protein Engineering, Vol. 13, No. 4, 253-258, April 2000
© 2000 Oxford University Press

Crystal structures of 3-isopropylmalate dehydrogenases with mutations at the C-terminus: crystallographic analyses of structure–stability relationships

Zeily Nurachman1, Satoshi Akanuma2, Takao Sato1, Tairo Oshima3 and Nobuo Tanaka1,4

1 Department of Life Science, Faculty of Bioscience and Biotechnology, Tokyo Institute of Technology, Nagatsuta 4259, Yokohama 226-8501, 2 Institute of Physical and Chemical Research (RIKEN), Wako 351-0198 and 3 Department of Molecular Biology, Tokyo University of Pharmacy and Life Science, Horinouchi, Hachioji 192-0392, Japan

Thermal stability of the Thermus thermophilus isopropylmalate dehydrogenase enzyme was substantially lost upon the deletion of three residues from the C-terminus. However, the stability was partly recovered by the addition of two, four and seven amino acid residues (called HD177, HD708 and HD711, respectively) to the C-terminal region of the truncated enzyme. Three structures of these mutant enzymes were determined by an X-ray diffraction method. All protein crystals belong to space group P21 and their structures were solved by a standard molecular replacement method where the original dimer structure of the A172L mutant was used as a search model. Thermal stability of these mutant enzymes is discussed based on the 3D structure with special attention to the width of the active-site groove and the minor groove, distortion of ß-sheet pillar structure and size of cavity in the domain–domain interface around the C-terminus. Our previous studies revealed that the thermal stability of isopropylmalate dehydrogenase increases when the active-site cleft is closed (the closed form). In the present study it is shown that the active-site cleft can be regulated by open–close movement of the minor groove located at the opposite side to the active-site groove on the same subunit, through a paperclip-like motion.


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