Structural insights into conserved l-arabinose metabolic enzymes reveal the substrate binding site of a thermophilic l-arabinose isomerase

Yong Jik Lee, Sang Jae Lee, Seong Bo Kim, Sang Jun Lee, Sung Haeng Lee, Dong Woo Lee

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

Structural genomics demonstrates that despite low levels of structural similarity of proteins comprising a metabolic pathway, their substrate binding regions are likely to be conserved. Herein based on the 3D-structures of the α/β-fold proteins involved in the ara operon, we attempted to predict the substrate binding residues of thermophilic Geobacillus stearothermophilus l-arabinose isomerase (GSAI) with no 3D-structure available. Comparison of the structures of l-arabinose catabolic enzymes revealed a conserved feature to form the substrate-binding modules, which can be extended to predict the substrate binding site of GSAI (i.e., D195, E261 and E333). Moreover, these data implicated that proteins in the l-arabinose metabolic pathway might retain their substrate binding niches as the modular structure through conserved molecular evolution even with totally different structural scaffolds.

Original languageEnglish
Pages (from-to)1064-1070
Number of pages7
JournalFEBS Letters
Volume588
Issue number6
DOIs
Publication statusPublished - 2014 Mar 18

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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