Snapshot of a Michaelis complex in a sulfuryl transfer reaction: Crystal structure of a mouse sulfotransferase, mSULT1D1, complexed with donor substrate and accepter substrate

Takamasa Teramoto; Yoichi Sakakibara; Ming Cheh Liu; Masahito Suiko; Makoto Kimura; Yoshimitsu Kakuta

doi:10.1016/j.bbrc.2009.03.146

Snapshot of a Michaelis complex in a sulfuryl transfer reaction: Crystal structure of a mouse sulfotransferase, mSULT1D1, complexed with donor substrate and accepter substrate

Takamasa Teramoto, Yoichi Sakakibara, Ming Cheh Liu, Masahito Suiko, Makoto Kimura, Yoshimitsu Kakuta

Molecular Biosciences

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

17 Citations (Scopus)

Abstract

We report the crystal structure of mouse sulfotransferase, mSULT1D1, complexed with donor substrate 3′-phosphoadenosine 5′-phosphosulfate and accepter substrate p-nitrophenol. The structure is the first report of the native Michaelis complex of sulfotransferase. In the structure, three proposed catalytic residues (Lys48, Lys106, and His108) were in proper positions for engaging in the sulfuryl transfer reaction. The data strongly support that the sulfuryl transfer reaction proceeds through an S_N2-like in-line displacement mechanism.

Original language	English
Pages (from-to)	83-87
Number of pages	5
Journal	Biochemical and Biophysical Research Communications
Volume	383
Issue number	1
DOIs	https://doi.org/10.1016/j.bbrc.2009.03.146
Publication status	Published - May 22 2009

All Science Journal Classification (ASJC) codes

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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10.1016/j.bbrc.2009.03.146

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Teramoto, T., Sakakibara, Y., Liu, M. C., Suiko, M., Kimura, M., & Kakuta, Y. (2009). Snapshot of a Michaelis complex in a sulfuryl transfer reaction: Crystal structure of a mouse sulfotransferase, mSULT1D1, complexed with donor substrate and accepter substrate. Biochemical and Biophysical Research Communications, 383(1), 83-87. https://doi.org/10.1016/j.bbrc.2009.03.146

Snapshot of a Michaelis complex in a sulfuryl transfer reaction: Crystal structure of a mouse sulfotransferase, mSULT1D1, complexed with donor substrate and accepter substrate. / Teramoto, Takamasa; Sakakibara, Yoichi; Liu, Ming Cheh et al.
In: Biochemical and Biophysical Research Communications, Vol. 383, No. 1, 22.05.2009, p. 83-87.

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

Teramoto, T, Sakakibara, Y, Liu, MC, Suiko, M, Kimura, M & Kakuta, Y 2009, 'Snapshot of a Michaelis complex in a sulfuryl transfer reaction: Crystal structure of a mouse sulfotransferase, mSULT1D1, complexed with donor substrate and accepter substrate', Biochemical and Biophysical Research Communications, vol. 383, no. 1, pp. 83-87. https://doi.org/10.1016/j.bbrc.2009.03.146

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abstract = "We report the crystal structure of mouse sulfotransferase, mSULT1D1, complexed with donor substrate 3′-phosphoadenosine 5′-phosphosulfate and accepter substrate p-nitrophenol. The structure is the first report of the native Michaelis complex of sulfotransferase. In the structure, three proposed catalytic residues (Lys48, Lys106, and His108) were in proper positions for engaging in the sulfuryl transfer reaction. The data strongly support that the sulfuryl transfer reaction proceeds through an SN2-like in-line displacement mechanism.",

author = "Takamasa Teramoto and Yoichi Sakakibara and Liu, {Ming Cheh} and Masahito Suiko and Makoto Kimura and Yoshimitsu Kakuta",

note = "Funding Information: This research was supported by the Grant-in-Aid for Scientific Research and the National Project on Protein Structural and Functional Analyses from the Ministry of Education, Culture, Sports, Science and Technology, Japan. ",

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AU - Kimura, Makoto

AU - Kakuta, Yoshimitsu

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Snapshot of a Michaelis complex in a sulfuryl transfer reaction: Crystal structure of a mouse sulfotransferase, mSULT1D1, complexed with donor substrate and accepter substrate

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