The importance of the Abn2 calcium cluster in the endo-1,5-arabinanase activity from Bacillus subtilis

C E McVey; B Correia; S Lahiri; D de Sanctis; Maria Arménia Carrondo; P F Lindley; Isabel Maria Godinho de Sá Nogueira; Cláudio Manuel Soares; Isabel Bento

doi:10.1007/s00775-014-1105-x

The importance of the Abn2 calcium cluster in the endo-1,5-arabinanase activity from Bacillus subtilis

C E McVey, B Correia, S Lahiri, D de Sanctis, Maria Arménia Carrondo, P F Lindley, Isabel Maria Godinho de Sá Nogueira, Cláudio Manuel Soares, Isabel Bento

Research output: Contribution to journal › Article

3 Citations (Scopus)

Abstract

Arabinanase is a glycosyl hydrolase that is able to cleave the glycosidic bonds of α-1,5-L-arabinan, releasing arabino-oligosaccharides and L-arabinose. The enzyme has two domains, an N-terminal catalytic domain with a characteristic β-propeller fold and a C-terminal domain whose function is unknown. A calcium ion, located near the catalytic site, serves to stabilize the N-terminal domain, but it has also been proposed to play a key role in the enzyme mechanism. The present work describes the structure of an inactive mutant of the wild-type enzyme (H318Q) and in which the calcium ion has been adventitiously replaced by nickel. These structural studies, together with functional and modelling studies, clearly support the role of the calcium ion in the overall reaction mechanism.

Original language	English
Pages (from-to)	505-13
Number of pages	9
Journal	Journal Of Biological Inorganic Chemistry
Volume	19
Issue number	4-5
DOIs	https://doi.org/10.1007/s00775-014-1105-x
Publication status	Published - Jun 2014

Keywords

Bacillus subtilis
Calcium
Catalysis
Catalytic Domain
Crystallography, X-Ray
Glycoside Hydrolases
Models, Molecular
Mutagenesis, Site-Directed
Substrate Specificity
Journal Article
Research Support, Non-U.S. Gov't

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McVey, C E ; Correia, B ; Lahiri, S ; de Sanctis, D ; Carrondo, Maria Arménia ; Lindley, P F ; Sá Nogueira, Isabel Maria Godinho de ; Soares, Cláudio Manuel ; Bento, Isabel. / The importance of the Abn2 calcium cluster in the endo-1,5-arabinanase activity from Bacillus subtilis. In: Journal Of Biological Inorganic Chemistry. 2014 ; Vol. 19, No. 4-5. pp. 505-13.

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abstract = "Arabinanase is a glycosyl hydrolase that is able to cleave the glycosidic bonds of α-1,5-L-arabinan, releasing arabino-oligosaccharides and L-arabinose. The enzyme has two domains, an N-terminal catalytic domain with a characteristic β-propeller fold and a C-terminal domain whose function is unknown. A calcium ion, located near the catalytic site, serves to stabilize the N-terminal domain, but it has also been proposed to play a key role in the enzyme mechanism. The present work describes the structure of an inactive mutant of the wild-type enzyme (H318Q) and in which the calcium ion has been adventitiously replaced by nickel. These structural studies, together with functional and modelling studies, clearly support the role of the calcium ion in the overall reaction mechanism.",

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The importance of the Abn2 calcium cluster in the endo-1,5-arabinanase activity from Bacillus subtilis. / McVey, C E; Correia, B; Lahiri, S; de Sanctis, D; Carrondo, Maria Arménia; Lindley, P F; Sá Nogueira, Isabel Maria Godinho de ; Soares, Cláudio Manuel ; Bento, Isabel.

In: Journal Of Biological Inorganic Chemistry, Vol. 19, No. 4-5, 06.2014, p. 505-13.

Research output: Contribution to journal › Article

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AU - Carrondo, Maria Arménia

AU - Lindley, P F

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AU - Soares, Cláudio Manuel

AU - Bento, Isabel

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KW - Catalysis

KW - Catalytic Domain

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KW - Substrate Specificity

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