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Microbiology
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- MicrobiologyOpen Access
SbnI is a free serine kinase that generates O-phospho-l-serine for staphyloferrin B biosynthesis in Staphylococcus aureus
Journal of Biological ChemistryVol. 293Issue 16p6147–6160Published online: February 26, 2018- Meghan M. Verstraete
- Cecilia Perez-Borrajero
- Kirstin L. Brown
- David E. Heinrichs
- Michael E.P. Murphy
Cited in Scopus: 10Staphyloferrin B (SB) is an iron-chelating siderophore produced by Staphylococcus aureus in invasive infections. Proteins for SB biosynthesis and export are encoded by the sbnABCDEFGHI gene cluster, in which SbnI, a member of the ParB/Srx superfamily, acts as a heme-dependent transcriptional regulator of the sbn locus. However, no structural or functional information about SbnI is available. Here, a crystal structure of SbnI revealed striking structural similarity to an ADP-dependent free serine kinase, SerK, from the archaea Thermococcus kodakarensis. - MicrobiologyOpen Access
A Heme-responsive Regulator Controls Synthesis of Staphyloferrin B in Staphylococcus aureus
Journal of Biological ChemistryVol. 291Issue 1p29–40Published online: November 3, 2015- Holly A. Laakso
- Cristina L. Marolda
- Tyler B. Pinter
- Martin J. Stillman
- David E. Heinrichs
Cited in Scopus: 31Staphylococcus aureus possesses a multitude of mechanisms by which it can obtain iron during growth under iron starvation conditions. It expresses an effective heme acquisition system (the iron-regulated surface determinant system), it produces two carboxylate-type siderophores staphyloferrin A and staphyloferrin B (SB), and it expresses transporters for many other siderophores that it does not synthesize. The ferric uptake regulator protein regulates expression of genes encoding all of these systems.