Merli, A.; Manikandan, K.; Gráczer, E.; Schuldt, L.; Singh, R.K.; Závodszky, P.; Vas, M.; Weiss, M.S. : Crystallization and preliminary X-ray diffraction analysis of various enzyme-substrate complexes of isopropylmalate dehydrogenase from Thermus thermophilus. Acta Crystallographica Section F - Structural Biology and Crystallization Communications 66 (2010), p. 738-743
10.1107/S174430911001626X
Abstract:
The Thermus thermophilus 3-isopropylmalate dehydrogenase (Tt-IPMDH) enzyme catalyses the penultimate step of the leucine-biosynthesis pathway. It converts (2R,3S)-3-isopropylmalate to (2S)-2-isopropyl-3-oxosuccinate in the presence of divalent Mg2+ or Mn2+ and with the help of NAD+. In order to elucidate the detailed structural and functional mode of the enzymatic reaction, crystals of Tt-IPMDH were grown in the presence of various combinations of substrate and/or cofactors. Here, the crystallization, data collection and preliminary crystallographic analyses of six such complexes are reported.