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 journalArticle

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 1

Fingerprint

galactose
Vibrio
Crystallization
Galactose
X-Rays
crystallization
X rays
Metabolic Networks and Pathways
enzymes
x rays
proteins
fermentation
Biofuels
metabolism
microorganisms
Enzymes
sugars
Substrate Specificity
Recombinant Proteins
structural analysis

Keywords

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

ASJC Scopus subject areas

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

Cite this

@article{419f8c6ff83a4cf3a863c09f9e864bd1,
title = "3,6-Anhydro-l-galactonate cycloisomerase from Vibrio sp. strain EJY3: Crystallization and X-ray crystallographic analysis",
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 {\AA} resolution and belonged to space group P41212 or P43212, with unit-cell parameters a = b = 87.9, c = 143.5 {\AA}. The Matthews coefficient was 2.3 {\AA}3 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.",
keywords = "3,6-anhydro-l-galactonate, 3,6-anhydro-l-galactonate cycloisomerase, 3,6-anhydro-l-galactose, ACI, agarolytic pathway, AHG metabolism, AHGA, Vibrio",
author = "Saeyoung Lee and Yun, {Eun Ju} and Kim, {Kyoung Heon} and Kim, {Hye Yeon} and In-Geol Choi",
year = "2017",
month = "9",
day = "1",
doi = "10.1107/S2053230X17011797",
language = "English",
volume = "73",
pages = "511--514",
journal = "Acta Crystallographica Section F:Structural Biology Communications",
issn = "1744-3091",
publisher = "John Wiley and Sons Ltd",
number = "9",

}

TY - JOUR

T1 - 3,6-Anhydro-l-galactonate cycloisomerase from Vibrio sp. strain EJY3

T2 - Crystallization and X-ray crystallographic analysis

AU - Lee, Saeyoung

AU - Yun, Eun Ju

AU - Kim, Kyoung Heon

AU - Kim, Hye Yeon

AU - Choi, In-Geol

PY - 2017/9/1

Y1 - 2017/9/1

N2 - 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.

AB - 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.

KW - 3,6-anhydro-l-galactonate

KW - 3,6-anhydro-l-galactonate cycloisomerase

KW - 3,6-anhydro-l-galactose

KW - ACI

KW - agarolytic pathway

KW - AHG metabolism

KW - AHGA

KW - Vibrio

UR - http://www.scopus.com/inward/record.url?scp=85028826299&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85028826299&partnerID=8YFLogxK

U2 - 10.1107/S2053230X17011797

DO - 10.1107/S2053230X17011797

M3 - Article

C2 - 28876229

AN - SCOPUS:85028826299

VL - 73

SP - 511

EP - 514

JO - Acta Crystallographica Section F:Structural Biology Communications

JF - Acta Crystallographica Section F:Structural Biology Communications

SN - 1744-3091

IS - 9

ER -