ArticleThe Journal of biological chemistry2014
SbnG, a citrate synthase in Staphylococcus aureus: a new fold on an old enzyme.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 23 citations in OpenAlex.
- Pheno- and genotypic iron acquisition of non-aureus staphylococci: a scoping review of literature with a focus on bovine mastitis.Veterinary research · 2025Article
- Iron-based microbial interactions: the role of iron metabolism in the cheese ecosystem.Journal of bacteriology · 2025Review
- Iron Metabolism at the Interface between Host and Pathogen: From Nutritional Immunity to Antibacterial Development.International journal of molecular sciences · 2020Review
- The steroid side-chain-cleaving aldolase Ltp2-ChsH2The Journal of biological chemistry · 2019Article
- SbnI is a free serine kinase that generatesThe Journal of biological chemistry · 2018Article
- Siderophores in Iron Metabolism: From Mechanism to Therapy Potential.Trends in molecular medicine · 2016Review
- Deciphering the Substrate Specificity of SbnA, the Enzyme Catalyzing the First Step in Staphyloferrin B Biosynthesis.Biochemistry · 2016Article
- An active site-tail interaction in the structure of hexahistidine-tagged Thermoplasma acidophilum citrate synthase.Acta crystallographica. Section F, Structural biology communications · 2015Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
In response to iron deprivation, Staphylococcus aureus produces staphyloferrin B, a citrate-containing siderophore that delivers iron back to the cell. This bacterium also possesses a second citrate synthase, SbnG, that is necessary for supplying citrate to the staphyloferrin B biosynthetic pathway. We present the structure of SbnG bound to the inhibitor calcium and an active site variant in complex with oxaloacetate. The overall fold of SbnG is structurally distinct from TCA cycle citrate synthases yet similar to metal-dependent class II aldolases. Phylogenetic analyses revealed that SbnG forms a separate clade with homologs from other siderophore biosynthetic gene clusters and is representative of a metal-independent subgroup in the phosphoenolpyruvate/pyruvate domain superfamily. A structural superposition of the SbnG active site to TCA cycle citrate synthases and site-directed mutagenesis suggests a case for convergent evolution toward a conserved catalytic mechanism for citrate production.
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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.