Novel catalytic mechanism of glycoside hydrolysis based on the structure of an NAD+/Mn2+-dependent phospho-α-glucosidase from Bacillus subtilis

Shyamala S. Rajan; Xiaojing Yang; Frank Collart; Vivian L.Y. Yip; Stephen G. Withers; Annabelle Varrot; John Thompson; Gideon J. Davies; Wayne F. Anderson

doi:10.1016/j.str.2004.06.020

Novel catalytic mechanism of glycoside hydrolysis based on the structure of an NAD⁺/Mn²⁺-dependent phospho-α-glucosidase from Bacillus subtilis

Shyamala S. Rajan, Xiaojing Yang, Frank Collart, Vivian L.Y. Yip, Stephen G. Withers, Annabelle Varrot, John Thompson, Gideon J. Davies, Wayne F. Anderson^*

^*Corresponding author for this work

Biochemistry and Molecular Genetics

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

72 Scopus citations

Abstract

GlvA, a 6-phospho-α-glucosidase from Bacillus subtilis, catalyzes the hydrolysis of maltose-6′-phosphate and belongs to glycoside hydrolase family GH4. GH4 enzymes are unique in their requirement for NAD(H) and a divalent metal for activity. We have determined the crystal structure of GlvA in complex with its ligands to 2.05 Å resolution. Analyses of the active site architecture, in conjunction with mechanistic studies and precedent from the nucleotide diphosphate hexose dehydratases and other systems, suggest a novel mechanism of glycoside hydrolysis by GlvA that involves both the NAD(H) and the metal.

Original language	English (US)
Pages (from-to)	1619-1629
Number of pages	11
Journal	Structure
Volume	12
Issue number	9
DOIs	https://doi.org/10.1016/j.str.2004.06.020
State	Published - Sep 2004

ASJC Scopus subject areas

Structural Biology
Molecular Biology

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Rajan, Shyamala S. ; Yang, Xiaojing ; Collart, Frank ; Yip, Vivian L.Y. ; Withers, Stephen G. ; Varrot, Annabelle ; Thompson, John ; Davies, Gideon J. ; Anderson, Wayne F. / Novel catalytic mechanism of glycoside hydrolysis based on the structure of an NAD⁺/Mn²⁺-dependent phospho-α-glucosidase from Bacillus subtilis. In: Structure. 2004 ; Vol. 12, No. 9. pp. 1619-1629.

@article{87176b07171941c285f89397477f13c5,

title = "Novel catalytic mechanism of glycoside hydrolysis based on the structure of an NAD+/Mn2+-dependent phospho-α-glucosidase from Bacillus subtilis",

abstract = "GlvA, a 6-phospho-α-glucosidase from Bacillus subtilis, catalyzes the hydrolysis of maltose-6′-phosphate and belongs to glycoside hydrolase family GH4. GH4 enzymes are unique in their requirement for NAD(H) and a divalent metal for activity. We have determined the crystal structure of GlvA in complex with its ligands to 2.05 {\AA} resolution. Analyses of the active site architecture, in conjunction with mechanistic studies and precedent from the nucleotide diphosphate hexose dehydratases and other systems, suggest a novel mechanism of glycoside hydrolysis by GlvA that involves both the NAD(H) and the metal.",

author = "Rajan, {Shyamala S.} and Xiaojing Yang and Frank Collart and Yip, {Vivian L.Y.} and Withers, {Stephen G.} and Annabelle Varrot and John Thompson and Davies, {Gideon J.} and Anderson, {Wayne F.}",

note = "Funding Information: Diffraction data were collected at the DND-CAT Synchrotron Research Center (Sector 5-IDB) of the Advanced Photon Source. This work was supported by an NIH grant (GM62414) to the Midwest Center for Structural Genomics. Additional funding came from the R.H. Lurie Cancer Center of Northwestern University, the Natural Sciences and Engineering Research Council of Canada, Michael Smith Foundation for Health Research, and the Protein Engineering Network of Centres for Excellence of Canada. We thank D. Miller and L. Shuvalova for data collection, J. Brunzelle for assistance with computational methods, A. Pikis for experimental assistance, Y. Li and B. Henrissat for preliminary data, M. Zasadzki and V. Gurram in preparing some figures, and P. Focia for a critical review of this manuscript. ",

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Novel catalytic mechanism of glycoside hydrolysis based on the structure of an NAD⁺/Mn²⁺-dependent phospho-α-glucosidase from Bacillus subtilis. / Rajan, Shyamala S.; Yang, Xiaojing; Collart, Frank; Yip, Vivian L.Y.; Withers, Stephen G.; Varrot, Annabelle; Thompson, John; Davies, Gideon J.; Anderson, Wayne F.

In: Structure, Vol. 12, No. 9, 09.2004, p. 1619-1629.

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

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AU - Rajan, Shyamala S.

AU - Yang, Xiaojing

AU - Collart, Frank

AU - Yip, Vivian L.Y.

AU - Withers, Stephen G.

AU - Varrot, Annabelle

AU - Thompson, John

AU - Davies, Gideon J.

AU - Anderson, Wayne F.

N1 - Funding Information: Diffraction data were collected at the DND-CAT Synchrotron Research Center (Sector 5-IDB) of the Advanced Photon Source. This work was supported by an NIH grant (GM62414) to the Midwest Center for Structural Genomics. Additional funding came from the R.H. Lurie Cancer Center of Northwestern University, the Natural Sciences and Engineering Research Council of Canada, Michael Smith Foundation for Health Research, and the Protein Engineering Network of Centres for Excellence of Canada. We thank D. Miller and L. Shuvalova for data collection, J. Brunzelle for assistance with computational methods, A. Pikis for experimental assistance, Y. Li and B. Henrissat for preliminary data, M. Zasadzki and V. Gurram in preparing some figures, and P. Focia for a critical review of this manuscript.

PY - 2004/9

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N2 - GlvA, a 6-phospho-α-glucosidase from Bacillus subtilis, catalyzes the hydrolysis of maltose-6′-phosphate and belongs to glycoside hydrolase family GH4. GH4 enzymes are unique in their requirement for NAD(H) and a divalent metal for activity. We have determined the crystal structure of GlvA in complex with its ligands to 2.05 Å resolution. Analyses of the active site architecture, in conjunction with mechanistic studies and precedent from the nucleotide diphosphate hexose dehydratases and other systems, suggest a novel mechanism of glycoside hydrolysis by GlvA that involves both the NAD(H) and the metal.

AB - GlvA, a 6-phospho-α-glucosidase from Bacillus subtilis, catalyzes the hydrolysis of maltose-6′-phosphate and belongs to glycoside hydrolase family GH4. GH4 enzymes are unique in their requirement for NAD(H) and a divalent metal for activity. We have determined the crystal structure of GlvA in complex with its ligands to 2.05 Å resolution. Analyses of the active site architecture, in conjunction with mechanistic studies and precedent from the nucleotide diphosphate hexose dehydratases and other systems, suggest a novel mechanism of glycoside hydrolysis by GlvA that involves both the NAD(H) and the metal.

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