ArticleProtein science : a publication of the Protein Society2007
Active site geometry of glucose-1-phosphate uridylyltransferase.
Article in Protein science : a publication of the Protein Society, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed.
- Article
- Van der Waals interactions mediate the enantiomeric substrate preference of the CTP:phosphoglycerate cytidylyltransferase CpgD.bioRxiv : the preprint server for biology · 2026Article
- The post-reactive structures ofMicrobiology spectrum · 2025Article
- Identification and characterization of the functional tetrameric UDP-glucose pyrophosphorylase frommBio · 2025Article
- Architecture, Function, Regulation, and Evolution of α-Glucans Metabolic Enzymes in Prokaryotes.Chemical reviews · 2024Review
- Article
- Article
- Single-molecule investigations of single-chain cellulose biosynthesis.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Heterologous expression and biological characteristics of UGPases from Lactobacillus acidophilus.Applied microbiology and biotechnology · 2022Article
- Production of bacterial cellulose from glycerol: the current state and perspectives.Bioresources and bioprocessing · 2021Review
- A mechanism-inspired UDP-RSC chemical biology · 2020Article
- Article
- Two Homologous Enzymes of the GalU Family inInternational journal of molecular sciences · 2019Article
- Crystal structure of UDP-glucose pyrophosphorylase from Yersinia pestis, a potential therapeutic target against plague.Acta crystallographica. Section F, Structural biology communications · 2019Article
- Phosphoribosyl Diphosphate (PRPP): Biosynthesis, Enzymology, Utilization, and Metabolic Significance.Microbiology and molecular biology reviews : MMBR · 2017Review
- Structures of aminoarabinose transferase ArnT suggest a molecular basis for lipid A glycosylation.Science (New York, N.Y.) · 2016Article
- On the Ancestral UDP-Glucose Pyrophosphorylase Activity of GalF from Escherichia coli.Frontiers in microbiology · 2015Article
- Expression, purification, crystallization and preliminary X-ray analysis of glucose-1-phosphate uridylyltransferase (GalU) from Erwinia amylovora.Acta crystallographica. Section F, Structural biology communications · 2014Article
- CugP is a novel ubiquitous non-GalU-type bacterial UDP-glucose pyrophosphorylase found in cyanobacteria.Journal of bacteriology · 2014Article
- Article
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2 authors.
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Abstract
Glucose-1-phosphate uridylyltransferase, or UGPase, catalyzes the production of UDP-glucose from glucose-1-phosphate and UTP. Because of the biological role of UDP-glucose in glycogen synthesis and in the formation of glycolipids, glycoproteins, and proteoglycans, the enzyme is widespread in nature. Recently this laboratory reported the three-dimensional structure of UGPase from Escherichia coli. While the initial X-ray analysis revealed the overall fold of the enzyme, details concerning its active site geometry were limited because crystals of the protein complexed with either substrates or products could never be obtained. In an effort to more fully investigate the active site geometry of the enzyme, UGPase from Corynebacterium glutamicum was subsequently cloned and purified. Here we report the X-ray structure of UGPase crystallized in the presence of both magnesium and UDP-glucose. Residues involved in anchoring the ligand to the active site include the polypeptide chain backbone atoms of Ala 20, Gly 21, Gly 117, Gly 180, and Ala 214, and the side chains of Glu 36, Gln 112, Asp 143, Glu 201, and Lys 202. Two magnesium ions are observed coordinated to the UDP-glucose. An alpha- and a beta-phosphoryl oxygen, three waters, and the side chain of Asp 142 ligate the first magnesium, whereas the second ion is coordinated by an alpha-phosphoryl oxygen and five waters. The position of the first magnesium is conserved in both the glucose-1-phosphate thymidylyltransferases and the cytidylyltransferases. The structure presented here provides further support for the role of the conserved magnesium ion in the catalytic mechanisms of the sugar-1-phosphate nucleotidylyltransferases.
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