ArticleJournal of molecular biology2009
Ligand binding and substrate discrimination by UDP-galactopyranose mutase.
Article in Journal of molecular biology, 2009. 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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Who cites it
28 citing papers in PubMed, 49 citations in OpenAlex.
- Structural bioinformatics insights into UDP-galactopyranose mutase (UGM) as a novel drug target for antifilarial therapy against human filarial parasite Brugia malayi.Molecular diversity · 2026Article
- The role and application of bioinformatics techniques and tools in drug discovery.Frontiers in pharmacology · 2025Review
- Targeting the Conformational Change in ArnA Dehydrogenase for Selective Inhibition of Polymyxin Resistance.Biochemistry · 2023Article
- N5 Is the New C4a: Biochemical Functionalization of Reduced Flavins at the N5 Position.Frontiers in molecular biosciences · 2020Review
- Molecular Dynamics Simulations of Substrate Release from Trypanosoma cruzi UDP-Galactopyranose Mutase.Journal of chemical information and modeling · 2019Article
- Antimycobacterial, Enzyme Inhibition, and Molecular Interaction Studies of Psoromic Acid inJournal of clinical medicine · 2018Article
- Steric Control of the Rate-Limiting Step of UDP-Galactopyranose Mutase.Biochemistry · 2018Article
- Deciphering the sugar biosynthetic pathway and tailoring steps of nucleoside antibiotic A201A unveils a GDP-l-galactose mutase.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Bioinformatics and Drug Discovery.Current topics in medicinal chemistry · 2017Review
- Virtual Screening for UDP-Galactopyranose Mutase Ligands Identifies a New Class of Antimycobacterial Agents.ACS chemical biology · 2015Article
- Agrobacterium tumefaciens exoR controls acid response genes and impacts exopolysaccharide synthesis, horizontal gene transfer, and virulence gene expression.Journal of bacteriology · 2014Article
- Structure, mechanism, and dynamics of UDP-galactopyranose mutase.Archives of biochemistry and biophysics · 2014Review
- Article
- UDP-galactopyranose mutase in nematodes.Biochemistry · 2013Article
- Characterization of the 5-hydroxymethylcytosine-specific DNA restriction endonucleases.Nucleic acids research · 2013Article
- Targeting UDP-galactopyranose mutases from eukaryotic human pathogens.Current pharmaceutical design · 2013Review
- Identification of the NAD(P)H binding site of eukaryotic UDP-galactopyranose mutase.Journal of the American Chemical Society · 2012Article
- The structural biology of enzymes involved in natural product glycosylation.Natural product reports · 2012Review
- Crystal structures of Trypanosoma cruzi UDP-galactopyranose mutase implicate flexibility of the histidine loop in enzyme activation.Biochemistry · 2012Article
- Purification, crystallization and preliminary X-ray diffraction data of UDP-galactopyranose mutase from Aspergillus fumigatus.Acta crystallographica. Section F, Structural biology and crystallization communications · 2012Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Galactofuranose (Galf) residues are present in cell wall glycoconjugates of numerous pathogenic microbes. Uridine 5'-diphosphate (UDP) Galf, the biosynthetic precursor of Galf-containing glycoconjugates, is produced from UDP-galactopyranose (UDP-Galp) by the flavoenzyme UDP-galactopyranose mutase (UGM). The gene encoding UGM (glf) is essential for the viability of pathogens, including Mycobacterium tuberculosis, and this finding underscores the need to understand how UGM functions. Considerable effort has been devoted to elucidating the catalytic mechanism of UGM, but progress has been hindered by a lack of structural data for an enzyme-substrate complex. Such data could reveal not only substrate binding interactions but how UGM can act preferentially on two very different substrates, UDP-Galp and UDP-Galf, yet avoid other structurally related UDP sugars present in the cell. Herein, we describe the first structure of a UGM-ligand complex, which provides insight into the catalytic mechanism and molecular basis for substrate selectivity. The structure of UGM from Klebsiella pneumoniae bound to the substrate analog UDP-glucose (UDP-Glc) was solved by X-ray crystallographic methods and refined to 2.5 A resolution. The ligand is proximal to the cofactor, a finding that is consistent with a proposed mechanism in which the reduced flavin engages in covalent catalysis. Despite this proximity, the glucose ring of the substrate analog is positioned such that it disfavors covalent catalysis. This orientation is consistent with data indicating that UDP-Glc is not a substrate for UGM. The relative binding orientations of UDP-Galp and UDP-Glc were compared using saturation transfer difference NMR. The results indicate that the uridine moiety occupies a similar location in both ligand complexes, and this relevant binding mode is defined by our structural data. In contrast, the orientations of the glucose and galactose sugar moieties differ. To understand the consequences of these differences, we derived a model for the productive UGM-substrate complex that highlights interactions that can contribute to catalysis and substrate discrimination.
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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.