D
IPR048652

Iron-regulated surface determinant protein H/B, linker domain

InterPro entry
Short nameIsd_H_B_linker

Description

The bacterial pathogen Staphylococcus aureus uses two closely related receptors located on its surface, IsdH and IsdB, to capture from haemoglobin (Hb) the iron it needs to grow. Both proteins show conserved near iron transporter (NEAT) domains (
IPR006635
) that function synergistically. These domains, essential for the arrest of iron, are appropriately positioned by an α-helical linker domain (this entry), which does not interact with the heme group. In IsdH, this linker domain forms a three-helix bundle structure that is essential for efficient heme capture
[1, 2, 3, 4]
.

References

1.Staphylococcus aureus uses a novel multidomain receptor to break apart human hemoglobin and steal its heme. Spirig T, Malmirchegini GR, Zhang J, Robson SA, Sjodt M, Liu M, Krishna Kumar K, Dickson CF, Gell DA, Lei B, Loo JA, Clubb RT. J Biol Chem 288, 1065-78, (2013). View articlePMID: 23132864

2.Structure of the hemoglobin-IsdH complex reveals the molecular basis of iron capture by Staphylococcus aureus. Dickson CF, Kumar KK, Jacques DA, Malmirchegini GR, Spirig T, Mackay JP, Clubb RT, Guss JM, Gell DA. J Biol Chem 289, 6728-6738, (2014). View articlePMID: 24425866

3.The structure of haemoglobin bound to the haemoglobin receptor IsdH from Staphylococcus aureus shows disruption of the native α-globin haem pocket. Dickson CF, Jacques DA, Clubb RT, Guss JM, Gell DA. Acta Crystallogr D Biol Crystallogr 71, 1295-306, (2015). View articlePMID: 26057669

4.Structure-function analyses reveal key features in <i>Staphylococcus aureus</i> IsdB-associated unfolding of the heme-binding pocket of human hemoglobin. Bowden CFM, Chan ACK, Li EJW, Arrieta AL, Eltis LD, Murphy MEP. J Biol Chem 293, 177-190, (2018). View articlePMID: 29109153

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