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3,6-Anhydro-L-galactonate cycloisomerase from Vibrio sp strain EJY3: crystallization and X-ray crystallographic analysis

Authors
Lee, SaeyoungYun, Eun JuKim, Kyoung HeonKim, Hye-YeonChoi, In-Geol
Issue Date
9월-2017
Publisher
INT UNION CRYSTALLOGRAPHY
Keywords
3,6-anhydro-L-galactonate; AHGA; 3,6-anhydro-L-galactonate cycloisomerase; ACI; AHG metabolism; agarolytic pathway; 3,6-anhydro-L-galactose; Vibrio
Citation
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, v.73, pp.511 - 514
Indexed
SCIE
SCOPUS
Journal Title
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
Volume
73
Start Page
511
End Page
514
URI
https://scholar.korea.ac.kr/handle/2021.sw.korea/82396
DOI
10.1107/S2053230X17011797
ISSN
2053-230X
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 angstrom resolution and belonged to space group P4(1)2(1)2 or P4(3)2(1)2, with unit-cell parameters a = b = 87.9, c = 143.5 angstrom. The Matthews coefficient was 2.3 angstrom 3 Da(-1), with a solvent content of 47%.
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