期刊
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
卷 73, 期 -, 页码 511-514出版社
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S2053230X17011797
关键词
3,6-anhydro-L-galactonate; AHGA; 3,6-anhydro-L-galactonate cycloisomerase; ACI; AHG metabolism; agarolytic pathway; 3,6-anhydro-L-galactose; Vibrio
资金
- Ministry of Trade, Industry and Energy, Republic of Korea [10052721]
- Korea Basic Science Institute [C37969, T37230, T37412]
- National Research Council of Science and Technology (NST) [CRC-16-01-KRICT]
- Center for C1 Gas Refinery through the National Research Foundation of Korea [NRF-2015M3D3A1A01064883]
- Korea Evaluation Institute of Industrial Technology (KEIT) [10052721] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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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