ArticleThe Plant cell2005
The structure of a cyanobacterial sucrose-phosphatase reveals the sugar tongs that release free sucrose in the cell.
Article in The Plant cell, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
28 citing papers in PubMed, 67 citations in OpenAlex.
- Genome-Wide Analysis of Trehalose-6-Phosphate Phosphatases (TPP) Gene Family in Potato (Plants (Basel, Switzerland) · 2025Article
- Revealing elusive conformations of sucrose from hydrogen bond J-coupling in HMagnetic resonance in chemistry : MRC · 2024Article
- TheMolecular breeding : new strategies in plant improvement · 2024Article
- Architecture, Function, Regulation, and Evolution of α-Glucans Metabolic Enzymes in Prokaryotes.Chemical reviews · 2024Review
- The conserved crown bridge loop at the catalytic centre of enzymes of the haloacid dehalogenase superfamily.Current research in structural biology · 2023Article
- Cyanobacteria as cell factories for the photosynthetic production of sucrose.Frontiers in microbiology · 2023Review
- Sucrose-phosphate phosphatase from sugarcane reveals an ancestral tandem duplication.BMC plant biology · 2021Article
- Mapping the bacterial metabolic niche space.Nature communications · 2020Article
- A Highly EfficientPlant communications · 2020Article
- Functional Features of TREHALOSE-6-PHOSPHATE SYNTHASE1, an Essential Enzyme in Arabidopsis.The Plant cell · 2020Article
- Freshwater CyanobacteriumApplied and environmental microbiology · 2020Article
- Co-crystal Structure ofFrontiers in microbiology · 2020Article
- The Response Regulator Slr1588 RegulatesFrontiers in microbiology · 2017Article
- Structures of trehalose-6-phosphate phosphatase from pathogenic fungi reveal the mechanisms of substrate recognition and catalysis.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Article
- Cap-domain closure enables diverse substrate recognition by the C2-type haloacid dehalogenase-like sugar phosphatase Plasmodium falciparum HAD1.Acta crystallographica. Section D, Biological crystallography · 2015Article
- Sucrose in cyanobacteria: from a salt-response molecule to play a key role in nitrogen fixation.Life (Basel, Switzerland) · 2015Review
- Structure of the trehalose-6-phosphate phosphatase from Brugia malayi reveals key design principles for anthelmintic drugs.PLoS pathogens · 2014Article
- A trehalose-6-phosphate synthase gene from Saccharina japonica (Laminariales, Phaeophyceae).Molecular biology reports · 2014Article
- Conformations of the apo-, substrate-bound and phosphate-bound ATP-binding domain of the Cu(II) ATPase CopB illustrate coupling of domain movement to the catalytic cycle.Bioscience reports · 2012Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Sucrose-phosphatase (SPP) catalyzes the final step in the pathway of sucrose biosynthesis in both plants and cyanobacteria, and the SPPs from these two groups of organisms are closely related. We have crystallized the enzyme from the cyanobacterium Synechocystis sp PCC 6803 and determined its crystal structure alone and in complex with various ligands. The protein consists of a core domain containing the catalytic site and a smaller cap domain that contains a glucose binding site. Two flexible hinge loops link the two domains, forming a structure that resembles a pair of sugar tongs. The glucose binding site plays a major role in determining the enzyme's remarkable substrate specificity and is also important for its inhibition by sucrose and glucose. It is proposed that the catalytic reaction is initiated by nucleophilic attack on the substrate by Asp9 and involves formation of a covalent phospho-Asp9-enzyme intermediate. From modeling based on the SPP structure, we predict that the noncatalytic SPP-like domain of the Synechocystis sucrose-phosphate synthase could bind sucrose-6(F)-phosphate and propose that this domain might be involved in metabolite channeling between the last two enzymes in the pathway of sucrose synthesis.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.