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PDBsum entry 4ij2

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protein ligands Protein-protein interface(s) links
Oxygen transport/protein binding PDB id
4ij2
Jmol PyMol
Contents
Protein chains
139 a.a.
146 a.a.
300 a.a.
197 a.a.
Ligands
HEM ×4
PDB id:
4ij2
Name: Oxygen transport/protein binding
Title: Human methemoglobin in complex with the second and third nea of isdh from staphylococcus aureus
Structure: Hemoglobin subunit alpha. Chain: a, c. Synonym: alpha-globin, hemoglobin alpha chain. Hemoglobin subunit beta. Chain: b, d. Synonym: beta-globin, hemoglobin beta chain, lvv-hemorphin- iron-regulated surface determinant protein h. Chain: e, f, g, h. Fragment: neat2, neat3, unp residues 326-660.
Source: Homo sapiens. Human. Organism_taxid: 9606. Tissue: red blood cells. Staphylococcus aureus. Organism_taxid: 367830. Strain: usa300. Gene: isdh. Expressed in: escherichia coli.
Resolution:
4.24Å     R-factor:   0.300     R-free:   0.310
Authors: C.F.Dickson,D.A.Jacques,J.M.Guss,D.A.Gell
Key ref: C.F.Dickson et al. (2014). Structure of the hemoglobin-IsdH complex reveals the molecular basis of iron capture by Staphylococcus aureus. J Biol Chem, 289, 6728-6738. PubMed id: 24425866 DOI: 10.1074/jbc.M113.545566
Date:
21-Dec-12     Release date:   25-Dec-13    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P69905  (HBA_HUMAN) -  Hemoglobin subunit alpha
Seq:
Struc:
142 a.a.
139 a.a.
Protein chains
Pfam   ArchSchema ?
P68871  (HBB_HUMAN) -  Hemoglobin subunit beta
Seq:
Struc:
147 a.a.
146 a.a.
Protein chains
Pfam   ArchSchema ?
Q2FG07  (ISDH_STAA3) -  Iron-regulated surface determinant protein H
Seq:
Struc:
 
Seq:
Struc:
895 a.a.
300 a.a.
Protein chain
Pfam   ArchSchema ?
Q2FG07  (ISDH_STAA3) -  Iron-regulated surface determinant protein H
Seq:
Struc:
 
Seq:
Struc:
895 a.a.
197 a.a.
Key:    PfamA domain  Secondary structure

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   11 terms 
  Biological process     transport   17 terms 
  Biochemical function     protein binding     9 terms  

 

 
DOI no: 10.1074/jbc.M113.545566 J Biol Chem 289:6728-6738 (2014)
PubMed id: 24425866  
 
 
Structure of the hemoglobin-IsdH complex reveals the molecular basis of iron capture by Staphylococcus aureus.
C.F.Dickson, K.K.Kumar, D.A.Jacques, G.R.Malmirchegini, T.Spirig, J.P.Mackay, R.T.Clubb, J.M.Guss, D.A.Gell.
 
  ABSTRACT  
 
Staphylococcus aureus causes life-threatening disease in humans. The S. aureus surface protein iron-regulated surface determinant H (IsdH) binds to mammalian hemoglobin (Hb) and extracts heme as a source of iron, which is an essential nutrient for the bacteria. However, the process of heme transfer from Hb is poorly understood. We have determined the structure of IsdH bound to human Hb by x-ray crystallography at 4.2 Å resolution, revealing the structural basis for heme transfer. One IsdH molecule is bound to each α and β Hb subunit, suggesting that the receptor acquires iron from both chains by a similar mechanism. Remarkably, two near iron transporter (NEAT) domains in IsdH perform very different functions. An N-terminal NEAT domain binds α/β globin through a site distant from the globin heme pocket and, via an intervening structural domain, positions the C-terminal heme-binding NEAT domain perfectly for heme transfer. These data, together with a 2.3 Å resolution crystal structure of the isolated N-terminal domain bound to Hb and small-angle x-ray scattering of free IsdH, reveal how multiple domains of IsdH cooperate to strip heme from Hb. Many bacterial pathogens obtain iron from human hemoglobin using proteins that contain multiple NEAT domains and other domains whose functions are poorly understood. Our results suggest that, rather than acting as isolated units, NEAT domains may be integrated into higher order architectures that employ multiple interaction interfaces to efficiently extract heme from host proteins.
 

 

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