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 › peer-review

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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10.1007/s00775-014-1105-x

Cite this

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.",

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",

author = "McVey, {C E} and B Correia and S Lahiri and {de Sanctis}, D and Carrondo, {Maria Arm{\'e}nia} and Lindley, {P F} and {S{\'a} Nogueira}, {Isabel Maria Godinho de} and Soares, {Cl{\'a}udio Manuel} and Isabel Bento",

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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 › peer-review

TY - JOUR

T1 - The importance of the Abn2 calcium cluster in the endo-1,5-arabinanase activity from Bacillus subtilis

AU - McVey, C E

AU - Correia, B

AU - Lahiri, S

AU - de Sanctis, D

AU - Carrondo, Maria Arménia

AU - Lindley, P F

AU - Sá Nogueira, Isabel Maria Godinho de

AU - Soares, Cláudio Manuel

AU - Bento, Isabel

N1 - WOS:000336310000003

PY - 2014/6

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N2 - 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.

AB - 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.

KW - Bacillus subtilis

KW - Calcium

KW - Catalysis

KW - Catalytic Domain

KW - Crystallography, X-Ray

KW - Glycoside Hydrolases

KW - Models, Molecular

KW - Mutagenesis, Site-Directed

KW - Substrate Specificity

KW - Journal Article

KW - Research Support, Non-U.S. Gov't

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DO - 10.1007/s00775-014-1105-x

M3 - Article

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VL - 19

SP - 505

EP - 513

JO - Journal Of Biological Inorganic Chemistry

JF - Journal Of Biological Inorganic Chemistry

SN - 0949-8257

IS - 4-5

ER -

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

Abstract

Keywords

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