Crystallization and preliminary X-ray diffraction analysis of various enzyme-substrate complexes of isopropylmalate dehydrogenase from Thermus thermophilus

Angelo Merli, Karuppasamy Manikandan, V. Gráczer, Linda Schuldt, Rajesh Kumar Singh, Péter Závodszky, Mária Vas, Manfred S. Weiss

Research output: Contribution to journalArticle

1 Citation (Scopus)

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 - oxo-succinate 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.

Original languageEnglish
Pages (from-to)738-743
Number of pages6
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume66
Issue number6
DOIs
Publication statusPublished - Jun 10 2010

Keywords

  • Isopropylmalate dehydrogenase
  • Leucine-biosynthesis pathway
  • Thermus thermophilus

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Genetics
  • Condensed Matter Physics

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