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Title: The Structure of Sucrose Phosphate Synthase from Halothermothrix orenii Reveals Its Mechanism of Action and Binding Mode

Abstract

Sucrose phosphate synthase (SPS) catalyzes the transfer of a glycosyl group from an activated donor sugar, such as uridine diphosphate glucose (UDP-Glc), to a saccharide acceptor D-fructose 6-phosphate (F6P), resulting in the formation of UDP and D-sucrose-6'-phosphate (S6P). This is a central regulatory process in the production of sucrose in plants, cyanobacteria, and proteobacteria. Here, we report the crystal structure of SPS from the nonphotosynthetic bacterium Halothermothrix orenii and its complexes with the substrate F6P and the product S6P. SPS has two distinct Rossmann-fold domains with a large substrate binding cleft at the interdomain interface. Structures of two complexes show that both the substrate F6P and the product S6P bind to the A-domain of SPS. Based on comparative analysis of the SPS structure with other related enzymes, the donor substrate, nucleotide diphosphate glucose, binds to the B-domain of SPS. Furthermore, we propose a mechanism of catalysis by H. orenii SPS. Our findings indicate that SPS from H. orenii may represent a valid model for the catalytic domain of plant SPSs and thus may provide useful insight into the reaction mechanism of the plant enzyme.

Authors:
; ; ; ; ; ; ; ;
Publication Date:
Research Org.:
Brookhaven National Lab. (BNL), Upton, NY (United States). National Synchrotron Light Source
Sponsoring Org.:
Doe - Office Of Science
OSTI Identifier:
960139
Report Number(s):
BNL-83125-2009-JA
TRN: US201016%%1283
DOE Contract Number:  
DE-AC02-98CH10886
Resource Type:
Journal Article
Journal Name:
The Plant Cell
Additional Journal Information:
Journal Volume: 20
Country of Publication:
United States
Language:
English
Subject:
36 MATERIALS SCIENCE; CATALYSIS; CRYSTAL STRUCTURE; CYANOBACTERIA; ENZYMES; GLUCOSE; NUCLEOTIDES; PHOSPHATES; PRODUCTION; REACTION KINETICS; SACCHARIDES; SACCHAROSE; SUBSTRATES; URIDINE; national synchrotron light source

Citation Formats

Chua, T, Bujnicki, J, Tan, T, Huynh, F, Patel, B, Sivaraman, J, Ogimoto, Y, Miyano, K, and Sawa, H. The Structure of Sucrose Phosphate Synthase from Halothermothrix orenii Reveals Its Mechanism of Action and Binding Mode. United States: N. p., 2008. Web. doi:10.1105/tpc.107.051193.
Chua, T, Bujnicki, J, Tan, T, Huynh, F, Patel, B, Sivaraman, J, Ogimoto, Y, Miyano, K, & Sawa, H. The Structure of Sucrose Phosphate Synthase from Halothermothrix orenii Reveals Its Mechanism of Action and Binding Mode. United States. https://doi.org/10.1105/tpc.107.051193
Chua, T, Bujnicki, J, Tan, T, Huynh, F, Patel, B, Sivaraman, J, Ogimoto, Y, Miyano, K, and Sawa, H. 2008. "The Structure of Sucrose Phosphate Synthase from Halothermothrix orenii Reveals Its Mechanism of Action and Binding Mode". United States. https://doi.org/10.1105/tpc.107.051193.
@article{osti_960139,
title = {The Structure of Sucrose Phosphate Synthase from Halothermothrix orenii Reveals Its Mechanism of Action and Binding Mode},
author = {Chua, T and Bujnicki, J and Tan, T and Huynh, F and Patel, B and Sivaraman, J and Ogimoto, Y and Miyano, K and Sawa, H},
abstractNote = {Sucrose phosphate synthase (SPS) catalyzes the transfer of a glycosyl group from an activated donor sugar, such as uridine diphosphate glucose (UDP-Glc), to a saccharide acceptor D-fructose 6-phosphate (F6P), resulting in the formation of UDP and D-sucrose-6'-phosphate (S6P). This is a central regulatory process in the production of sucrose in plants, cyanobacteria, and proteobacteria. Here, we report the crystal structure of SPS from the nonphotosynthetic bacterium Halothermothrix orenii and its complexes with the substrate F6P and the product S6P. SPS has two distinct Rossmann-fold domains with a large substrate binding cleft at the interdomain interface. Structures of two complexes show that both the substrate F6P and the product S6P bind to the A-domain of SPS. Based on comparative analysis of the SPS structure with other related enzymes, the donor substrate, nucleotide diphosphate glucose, binds to the B-domain of SPS. Furthermore, we propose a mechanism of catalysis by H. orenii SPS. Our findings indicate that SPS from H. orenii may represent a valid model for the catalytic domain of plant SPSs and thus may provide useful insight into the reaction mechanism of the plant enzyme.},
doi = {10.1105/tpc.107.051193},
url = {https://www.osti.gov/biblio/960139}, journal = {The Plant Cell},
number = ,
volume = 20,
place = {United States},
year = {Tue Jan 01 00:00:00 EST 2008},
month = {Tue Jan 01 00:00:00 EST 2008}
}