title: Structural and Biochemical Characterization of an Octameric Carbohydrate Acetylesterase from Sinorhizobium meliloti.
abstract: Carbohydrate acetylesterases, which have a highly specific role among plant-interacting bacterial species, remove the acetyl groups from plant carbohydrates. Here, we determined the crystal structure of Est24, an octameric carbohydrate acetylesterase from Sinorhizobium meliloti, at 1.45 Å resolution and investigated its biochemical properties. The structure of Est24 consisted of five parallel β strands flanked by α helices, which formed an octameric assembly with two distinct interfaces. The deacetylation activity of Est24 and its mutants around the substrate-binding pocket was investigated using several substrates, including glucose pentaacetate and acetyl alginate. Elucidation of the structure-function relationships of Est24 could provide valuable opportunities for biotechnological explorations.
authors.affiliation: Department of Molecular Cell Biology, Samsung Biomedical Research Institute, Sungkyunkwan University School of Medicine, Suwon, Korea.
authors.forename: Changsuk
authors.initials: C
authors.lastname: Oh
authors.affiliation: Department of Molecular Cell Biology, Samsung Biomedical Research Institute, Sungkyunkwan University School of Medicine, Suwon, Korea.|Department of Chemistry, College of Natural Sciences, Sookmyung Woman's University, Seoul, Korea.
authors.forename: Bum Han
authors.initials: BH
authors.lastname: Ryu
authors.affiliation: Department of Molecular Cell Biology, Samsung Biomedical Research Institute, Sungkyunkwan University School of Medicine, Suwon, Korea.|Department of Chemistry, College of Natural Sciences, Sookmyung Woman's University, Seoul, Korea.
authors.forename: Deu Rae
authors.initials: DR
authors.lastname: An
authors.affiliation: Department of Molecular Cell Biology, Samsung Biomedical Research Institute, Sungkyunkwan University School of Medicine, Suwon, Korea.
authors.forename: Duy Duc
authors.initials: DD
authors.lastname: Nguyen
authors.affiliation: Department of Molecular Cell Biology, Samsung Biomedical Research Institute, Sungkyunkwan University School of Medicine, Suwon, Korea.|Department of Chemistry, College of Natural Sciences, Sookmyung Woman's University, Seoul, Korea.
authors.forename: Wanki
authors.initials: W
authors.lastname: Yoo
authors.affiliation: Department of Molecular Cell Biology, Samsung Biomedical Research Institute, Sungkyunkwan University School of Medicine, Suwon, Korea.
authors.forename: Truc
authors.initials: T
authors.lastname: Kim
authors.affiliation: Department of Molecular Cell Biology, Samsung Biomedical Research Institute, Sungkyunkwan University School of Medicine, Suwon, Korea.
authors.forename: Tri Duc
authors.initials: TD
authors.lastname: Ngo
authors.affiliation: Department of Food Science and Biotechnology, Kyungsung University, Busan, Korea.
authors.forename: Hee Sook
authors.initials: HS
authors.lastname: Kim
authors.affiliation: Department of Molecular Cell Biology, Samsung Biomedical Research Institute, Sungkyunkwan University School of Medicine, Suwon, Korea.
authors.forename: Kyeong Kyu
authors.initials: KK
authors.lastname: Kim
authors.affiliation: Department of Chemistry, College of Natural Sciences, Sookmyung Woman's University, Seoul, Korea.
authors.forename: T Doohun
authors.initials: TD
authors.lastname: Kim
mesh_terms: D000115:Acetylesterase / Q000737:chemistry* / Q000378:metabolism*; D000595:Amino Acid Sequence; D001665:Binding Sites; D002241:Carbohydrates / Q000737:chemistry*; D018360:Crystallography, X-Ray; D004252:DNA Mutational Analysis; D007660:Ketoprofen / Q000378:metabolism; D050505:Mutant Proteins / Q000378:metabolism; D055503:Protein Multimerization; D017433:Protein Structure, Secondary; D016415:Sequence Alignment; D020539:Sequence Analysis, Protein; D016962:Sinorhizobium meliloti / Q000201:enzymology*; D013379:Substrate Specificity
chemical_list: D002241:Carbohydrates; D050505:Mutant Proteins; D007660:Ketoprofen; D000115:Acetylesterase
keywords: carbohydrate acetylesterase; site-directed mutagenesis