3,6-Anhydro-l-galactonate cycloisomerase from Vibrio sp. strain EJY3: Crystallization and X-ray crystallographic analysis

Saeyoung Lee, Eun Ju Yun, Kyoung Heon Kim, Hye Yeon Kim, In Geol Choi

Research output: Contribution to journalArticlepeer-review

Abstract

3,6-Anhydro-l-galactonate cycloisomerase (ACI), which is found in the marine bacterium Vibrio sp. strain EJY3, converts 3,6-anhydro-l-galactonate into 2-keto-3-deoxygalactonate. ACI is a key enzyme in the metabolic pathway of 3,6-anhydro-l-galactose (AHG). Study of AHG metabolism is important for the efficient fermentation of agar and biofuel production, because AHG is a sugar that is non-fermentable by commercial microorganisms. The aci gene from Vibrio sp. strain EJY3 was cloned, and the recombinant protein was overexpressed and crystallized in order to determine the structure and understand the function of the protein. The crystals diffracted to 2.2 Å resolution and belonged to space group P41212 or P43212, with unit-cell parameters a = b = 87.9, c = 143.5 Å. The Matthews coefficient was 2.3 Å3 Da-1, with a solvent content of 47%.3,6-Anhydro-l-galactonate cycloisomerase (ACI) is a second-step enzyme in the metabolic pathway of 3,6-anhydro-l-galactose. Structural analysis of ACI is crucial in order to elucidate its function, substrate specificity and reaction mechanism at the molecular level.

Original languageEnglish
Pages (from-to)511-514
Number of pages4
JournalActa Crystallographica Section:F Structural Biology Communications
Volume73
Issue number9
DOIs
Publication statusPublished - 2017 Sep

Keywords

  • 3,6-anhydro-l-galactonate
  • 3,6-anhydro-l-galactonate cycloisomerase
  • 3,6-anhydro-l-galactose
  • ACI
  • AHG metabolism
  • AHGA
  • Vibrio
  • agarolytic pathway

ASJC Scopus subject areas

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

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