ArticleBiophysical journal2007
Structure and molecular mechanism of Bacillus anthracis cofactor-independent phosphoglycerate mutase: a crucial enzyme for spores and growing cells of Bacillus species.
Article in Biophysical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 26 citations in OpenAlex.
- Core Proteome Subtractive Genomics Reveals Potential Therapeutic Targets in Bacillus anthracis.Current microbiology · 2026Article
- Comparative gut microbial enzyme functions in human amoebiasis: Implications for host-microbe interactions and veterinary parasitic models.Open veterinary journal · 2026Article
- The function of phosphoglycerate mutase 1 (PGAM1) and its role in diseases.Frontiers in molecular biosciences · 2026Review
- Exoproteomic analysis of two MLST clade 2 strains of Clostridioides difficile from Latin America reveal close similarities.Scientific reports · 2021Article
- Structural and Functional Characterization of the BcsG Subunit of the Cellulose Synthase in Salmonella typhimurium.Journal of molecular biology · 2018Article
- Macrocycle peptides delineate locked-open inhibition mechanism for microorganism phosphoglycerate mutases.Nature communications · 2017Article
- Identification of Genes Controlled by the Essential YycFG Two-Component System Reveals a Role for Biofilm Modulation inFrontiers in microbiology · 2017Article
- Cofactor independent phosphoglycerate mutase of Brugia malayi induces a mixed Th1/Th2 type immune response and inhibits larval development in the host.BioMed research international · 2014Article
- Expression, purification, crystallization and preliminary X-ray diffraction studies of phosphoglycerate mutase from Staphylococcus aureus NCTC8325.Acta crystallographica. Section F, Structural biology communications · 2014Article
- Cofactor-independent phosphoglycerate mutase from nematodes has limited druggability, as revealed by two high-throughput screens.PLoS neglected tropical diseases · 2014Article
- Unliganded structure of human bisphosphoglycerate mutase reveals side-chain movements induced by ligand binding.Acta crystallographica. Section F, Structural biology and crystallization communications · 2010Article
- Comparative enzymology in the alkaline phosphatase superfamily to determine the catalytic role of an active-site metal ion.Journal of molecular biology · 2008Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Phosphoglycerate mutases (PGMs) catalyze the isomerization of 2- and 3-phosphoglycerates and are essential for glucose metabolism in most organisms. This study reports the production, structure, and molecular dynamics analysis of Bacillus anthracis cofactor-independent PGM (iPGM). The three-dimensional structure of B. anthracis PGM is composed of two structural and functional domains, the phosphatase and transferase. The structural relationship between these two domains is different than in the B. stearothermophilus iPGM structure determined previously. However, the structures of the two domains of B. anthracis iPGM show a high degree of similarity to those in B. stearothermophilus iPGM. The novel domain arrangement in B. anthracis iPGM and the dynamic property of these domains is directly linked to the mechanism of enzyme catalysis, in which substrate binding is proposed to result in close association of the two domains. The structure of B. anthracis iPGM and the molecular dynamics of this structure provide unique insight into the mechanism of iPGM catalysis, in particular the roles of changes in coordination geometry of the enzyme's two bivalent metal ions and the regulation of this enzyme's activity by changes in intracellular pH during spore formation and germination in Bacillus species.
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