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PDBsum entry 3ipr

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protein metals Protein-protein interface(s) links
Transferase PDB id
3ipr

 

 

 

 

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Contents
Protein chains
(+ 0 more) 137 a.a. *
Metals
_CA ×10
Waters ×117
* Residue conservation analysis
PDB id:
3ipr
Name: Transferase
Title: Crystal structure of the enterococcus faecalis gluconate specific eiia phosphotransferase system component
Structure: Pts system, iia component. Chain: a, b, c, d, e, f. Engineered: yes. Other_details: gluconate specific eiia phosphotransferase system component from enterococcus faecalis
Source: Enterococcus faecalis. Organism_taxid: 1351. Strain: 26487 wildtype. Gene: ef_3136, gntf. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.50Å     R-factor:   0.189     R-free:   0.248
Authors: S.Reinelt,S.Welti,K.Scheffzek
Key ref: S.Reinelt et al. (2009). Structure of the Enterococcus faecalis EIIA(gnt) PTS component. Biochem Biophys Res Commun, 388, 626-629. PubMed id: 19682976
Date:
18-Aug-09     Release date:   15-Sep-09    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q82ZC8  (Q82ZC8_ENTFA) -  PTS system, IIA component from Enterococcus faecalis (strain ATCC 700802 / V583)
Seq:
Struc:
150 a.a.
137 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 

 
Biochem Biophys Res Commun 388:626-629 (2009)
PubMed id: 19682976  
 
 
Structure of the Enterococcus faecalis EIIA(gnt) PTS component.
S.Reinelt, B.Koch, M.Hothorn, W.Hengstenberg, S.Welti, K.Scheffzek.
 
  ABSTRACT  
 
In Eubacteria, the utilization of a number of extracellular carbohydrates is mediated by sugar specific phosphoenolepyruvate (PEP) dependent sugar phosphotransferase systems (PTSs), which simultaneously import und phosphorylate their target sugars. Here, we report the crystal structure of the EIIA(gnt) component of the so far little investigated Enterococcus faecalis gluconate specific PTS. The crystal structure shows a tightly interacting dimer of EIIA(gnt) which is structurally similar to the related EIIA(man) from Escherichia coli. Homology modeling of E. faecalis HPr, EIIB(man) and their complexes with EIIA(man) suggests that despite moderate sequence identity between EIIA(man) and EIIA(gnt), the active sites closely match the situation observed in the E. coli system with His-9 of EIIA(gnt) being the likely phosphoryl group carrier. We therefore propose that the phosphoryl transfer reactions involving EIIA(gnt) proceed according to a mechanism analog to the one described for E. coli EIIA(man).
 

 

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