Crystal Structures of Catalytic Intermediates of Human Selenophosphate Synthetase 1

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Crystal Structures of Catalytic Intermediates of Human Selenophosphate Synthetase 1. / Wang, Kai Tuo; Wang, Juan; Li, Lan Fen; Su, Xiao Dong.

In: Journal of Molecular Biology, Vol. 390, No. 4, 24.07.2009, p. 747-759.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Wang, KT, Wang, J, Li, LF & Su, XD 2009, 'Crystal Structures of Catalytic Intermediates of Human Selenophosphate Synthetase 1', Journal of Molecular Biology, vol. 390, no. 4, pp. 747-759. https://doi.org/10.1016/j.jmb.2009.05.032

APA

Wang, K. T., Wang, J., Li, L. F., & Su, X. D. (2009). Crystal Structures of Catalytic Intermediates of Human Selenophosphate Synthetase 1. Journal of Molecular Biology, 390(4), 747-759. https://doi.org/10.1016/j.jmb.2009.05.032

Vancouver

Wang KT, Wang J, Li LF, Su XD. Crystal Structures of Catalytic Intermediates of Human Selenophosphate Synthetase 1. Journal of Molecular Biology. 2009 Jul 24;390(4):747-759. https://doi.org/10.1016/j.jmb.2009.05.032

Author

Wang, Kai Tuo ; Wang, Juan ; Li, Lan Fen ; Su, Xiao Dong. / Crystal Structures of Catalytic Intermediates of Human Selenophosphate Synthetase 1. In: Journal of Molecular Biology. 2009 ; Vol. 390, No. 4. pp. 747-759.

Bibtex

@article{f5345a85d76640bebf4f049acf3588d3,
title = "Crystal Structures of Catalytic Intermediates of Human Selenophosphate Synthetase 1",
abstract = "Selenophosphate synthetase catalyzes the synthesis of the highly active selenium donor molecule selenophosphate, a key intermediate in selenium metabolism. We have determined the high-resolution crystal structure of human selenophosphate synthetase 1 (hSPS1). An unexpected reaction intermediate, with a tightly bound phosphate and ADP at the active site has been captured in the structure. An enzymatic assay revealed that hSPS1 possesses low ADP hydrolysis activity in the presence of phosphate. Our structural and enzymatic results suggest that consuming the second high-energy phosphoester bond of ATP could protect the labile product selenophosphate during catalytic reaction. We solved another hSPS1 structure with potassium ions at the active sites. Comparing the two structures, we were able to define the monovalent cation-binding site of the enzyme. The detailed mechanism of the ADP hydrolysis step and the exact function of the monovalent cation for hSPS1 catalytic reaction are proposed.",
keywords = "PurM superfamily, SelD, selenocysteine, SPS1",
author = "Wang, {Kai Tuo} and Juan Wang and Li, {Lan Fen} and Su, {Xiao Dong}",
year = "2009",
month = jul,
day = "24",
doi = "10.1016/j.jmb.2009.05.032",
language = "English",
volume = "390",
pages = "747--759",
journal = "Journal of Molecular Biology",
issn = "0022-2836",
publisher = "Academic Press",
number = "4",

}

RIS

TY - JOUR

T1 - Crystal Structures of Catalytic Intermediates of Human Selenophosphate Synthetase 1

AU - Wang, Kai Tuo

AU - Wang, Juan

AU - Li, Lan Fen

AU - Su, Xiao Dong

PY - 2009/7/24

Y1 - 2009/7/24

N2 - Selenophosphate synthetase catalyzes the synthesis of the highly active selenium donor molecule selenophosphate, a key intermediate in selenium metabolism. We have determined the high-resolution crystal structure of human selenophosphate synthetase 1 (hSPS1). An unexpected reaction intermediate, with a tightly bound phosphate and ADP at the active site has been captured in the structure. An enzymatic assay revealed that hSPS1 possesses low ADP hydrolysis activity in the presence of phosphate. Our structural and enzymatic results suggest that consuming the second high-energy phosphoester bond of ATP could protect the labile product selenophosphate during catalytic reaction. We solved another hSPS1 structure with potassium ions at the active sites. Comparing the two structures, we were able to define the monovalent cation-binding site of the enzyme. The detailed mechanism of the ADP hydrolysis step and the exact function of the monovalent cation for hSPS1 catalytic reaction are proposed.

AB - Selenophosphate synthetase catalyzes the synthesis of the highly active selenium donor molecule selenophosphate, a key intermediate in selenium metabolism. We have determined the high-resolution crystal structure of human selenophosphate synthetase 1 (hSPS1). An unexpected reaction intermediate, with a tightly bound phosphate and ADP at the active site has been captured in the structure. An enzymatic assay revealed that hSPS1 possesses low ADP hydrolysis activity in the presence of phosphate. Our structural and enzymatic results suggest that consuming the second high-energy phosphoester bond of ATP could protect the labile product selenophosphate during catalytic reaction. We solved another hSPS1 structure with potassium ions at the active sites. Comparing the two structures, we were able to define the monovalent cation-binding site of the enzyme. The detailed mechanism of the ADP hydrolysis step and the exact function of the monovalent cation for hSPS1 catalytic reaction are proposed.

KW - PurM superfamily

KW - SelD

KW - selenocysteine

KW - SPS1

UR - http://www.scopus.com/inward/record.url?scp=67649354030&partnerID=8YFLogxK

U2 - 10.1016/j.jmb.2009.05.032

DO - 10.1016/j.jmb.2009.05.032

M3 - Journal article

C2 - 19477186

AN - SCOPUS:67649354030

VL - 390

SP - 747

EP - 759

JO - Journal of Molecular Biology

JF - Journal of Molecular Biology

SN - 0022-2836

IS - 4

ER -

ID: 234874485