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PDBsum entry 3iby

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protein Protein-protein interface(s) links
Transport protein PDB id
3iby

 

 

 

 

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Contents
Protein chains
245 a.a. *
230 a.a. *
Waters ×117
* Residue conservation analysis
PDB id:
3iby
Name: Transport protein
Title: Structure of cytosolic domain of l. Pneumophila feob
Structure: Ferrous iron transport protein b. Chain: a, b, c, d. Fragment: cytosolic domain (unp residues 1-256). Engineered: yes
Source: Legionella pneumophila. Organism_taxid: 446. Gene: feob. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.50Å     R-factor:   0.216     R-free:   0.288
Authors: N.Petermann,G.Hansen,R.Hilgenfeld
Key ref: N.Petermann et al. (2010). Structure of the GTPase and GDI domains of FeoB, the ferrous iron transporter of Legionella pneumophila. Febs Lett, 584, 733-738. PubMed id: 20036663
Date:
17-Jul-09     Release date:   13-Oct-09    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q8GNS3  (FEOB_LEGPN) -  Fe(2+) transporter FeoB from Legionella pneumophila
Seq:
Struc:
 
Seq:
Struc:
751 a.a.
245 a.a.
Protein chain
Pfam   ArchSchema ?
Q8GNS3  (FEOB_LEGPN) -  Fe(2+) transporter FeoB from Legionella pneumophila
Seq:
Struc:
 
Seq:
Struc:
751 a.a.
230 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 

 
Febs Lett 584:733-738 (2010)
PubMed id: 20036663  
 
 
Structure of the GTPase and GDI domains of FeoB, the ferrous iron transporter of Legionella pneumophila.
N.Petermann, G.Hansen, C.L.Schmidt, R.Hilgenfeld.
 
  ABSTRACT  
 
Prokaryotic pathogens have developed specialized mechanisms for efficient uptake of ferrous iron (Fe(2+)) from the host. In Legionella pneumophila, the causative agent of Legionnaires' disease, the transmembrane GTPase FeoB plays a key role in Fe(2+) acquisition and virulence. FeoB consists of a membrane-embedded core and an N-terminal, cytosolic region (NFeoB). Here, we report the crystal structure of NFeoB from L. pneumophila, revealing a monomeric protein comprising two separate domains with GTPase and guanine-nucleotide dissociation inhibitor (GDI) functions. The GDI domain displays a novel fold, whereas the overall structure of the GTPase domain resembles that of known G domains but is in the rarely observed nucleotide-free state.
 

 

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