Crystal structure of LeuD from Methanococcus jannaschii

Eun Hye Lee, Yong Wook Cho, Kwang Yeon Hwang

Research output: Contribution to journalArticlepeer-review

6 Citations (Scopus)


3-Isopropylmalate/citramalate (IPM) isomerase catalyzes the second step in the leucine biosynthesis pathway. IPM isomerase from . Methanococcus jannaschii is a complex protein consisting of a large (MjLeuC) and a small subunit (MjLeuD). It has broad substrate specificity, unlike other bacterial IPM isomerases. In order to understand the reasons for this broad substrate specificity, we determined the crystal structure of . MjLeuD at a resolution of 2.0. å. The asymmetric unit contained 6 molecules of LeuD, including three homodimers. The overall structure had a β/β/α sandwich-fold consisting of 8 α-helices and 7 β-strands. The C-terminal helix, which is important in homodimer formation, showed conformational differences between two homodimer forms of . MjLeuD. In addition, we identified a hydrophobic residue (Val28) near the substrate recognition region that may explain the broad substrate specificity of IPM isomerase. Therefore, we suggest that LeuD proteins can be divided into 2 subfamilies, LeuD subfamilies 1 and 2, which show differences in overall structure and in the substrate recognition region.

Original languageEnglish
Pages (from-to)160-164
Number of pages5
JournalBiochemical and biophysical research communications
Issue number2
Publication statusPublished - 2012 Mar 9


  • 3-Isopropylmalate dehydratase
  • 3-Isopropylmalate isomerase
  • Broad specificity
  • Crystal structure
  • LeuD
  • Small subunit

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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