Structural and Biochemical Characterization of an Octameric Carbohydrate Acetylesterase from Sinorhizobium meliloti

Changsuk Oh; Bum Han Ryu; Deu Rae An; Duy Duc Nguyen; Wanki Yoo; Truc Kim; Tri Duc Ngo; Hee Sook Kim; Kyeong Kyu Kim; T. Doohun Kim

doi:10.1002/1873-3468.12135

Structural and Biochemical Characterization of an Octameric Carbohydrate Acetylesterase from Sinorhizobium meliloti

Changsuk Oh, Bum Han Ryu, Deu Rae An, Duy Duc Nguyen, Wanki Yoo, Truc Kim, Tri Duc Ngo, Hee Sook Kim, Kyeong Kyu Kim, T. Doohun Kim

Research output: Contribution to journal › Article › peer-review

17 Scopus citations

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.

Original language	English
Pages (from-to)	1242-1252
Number of pages	11
Journal	FEBS Letters
Volume	590
Issue number	8
DOIs	https://doi.org/10.1002/1873-3468.12135
State	Published - 1 Apr 2016
Externally published	Yes

Keywords

carbohydrate acetylesterase
site-directed mutagenesis

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10.1002/1873-3468.12135

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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 {\AA} 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.",

keywords = "carbohydrate acetylesterase, site-directed mutagenesis",

author = "Changsuk Oh and Ryu, \{Bum Han\} and An, \{Deu Rae\} and Nguyen, \{Duy Duc\} and Wanki Yoo and Truc Kim and Ngo, \{Tri Duc\} and Kim, \{Hee Sook\} and Kim, \{Kyeong Kyu\} and Kim, \{T. Doohun\}",

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doi = "10.1002/1873-3468.12135",

language = "English",

volume = "590",

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T1 - Structural and Biochemical Characterization of an Octameric Carbohydrate Acetylesterase from Sinorhizobium meliloti

AU - Oh, Changsuk

AU - Ryu, Bum Han

AU - An, Deu Rae

AU - Nguyen, Duy Duc

AU - Yoo, Wanki

AU - Kim, Truc

AU - Ngo, Tri Duc

AU - Kim, Hee Sook

AU - Kim, Kyeong Kyu

AU - Kim, T. Doohun

PY - 2016/4/1

Y1 - 2016/4/1

N2 - 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.

AB - 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.

KW - carbohydrate acetylesterase

KW - site-directed mutagenesis

UR - https://www.scopus.com/pages/publications/84962815867

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DO - 10.1002/1873-3468.12135

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JO - FEBS Letters

JF - FEBS Letters

IS - 8

ER -

Structural and Biochemical Characterization of an Octameric Carbohydrate Acetylesterase from Sinorhizobium meliloti

Abstract

Keywords

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