spacer
spacer

PDBsum entry 4hic

Go to PDB code: 
protein Protein-protein interface(s) links
Unknown function PDB id
4hic

 

 

 

 

Loading ...

 
JSmol PyMol  
Contents
Protein chains
204 a.a.
PDB id:
4hic
Name: Unknown function
Title: Crystal structure of the potential transfer protein trak from gram- positive conjugative plasmid pip501
Structure: Trak. Chain: a, b. Engineered: yes
Source: Enterococcus faecalis. Organism_taxid: 1351. Gene: orf11 from conjugative plasmid pip501. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Resolution:
3.00Å     R-factor:   0.213     R-free:   0.234
Authors: N.Goessweiner-Mohr,W.Keller
Key ref: N.Goessweiner-Mohr et al. (2014). The type IV secretion protein TraK from the Enterococcus conjugative plasmid pIP501 exhibits a novel fold. Acta Crystallogr D Biol Crystallogr, 70, 1124-1135. PubMed id: 24699656 DOI: 10.1107/S1399004714001606
Date:
11-Oct-12     Release date:   22-Jan-14    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Q8L1C9  (Q8L1C9_ENTFL) -  Sigma from Enterococcus faecalis
Seq:
Struc:
307 a.a.
204 a.a.
Key:    Secondary structure

 Enzyme reactions 
   Enzyme class: E.C.?
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

 

 
DOI no: 10.1107/S1399004714001606 Acta Crystallogr D Biol Crystallogr 70:1124-1135 (2014)
PubMed id: 24699656  
 
 
The type IV secretion protein TraK from the Enterococcus conjugative plasmid pIP501 exhibits a novel fold.
N.Goessweiner-Mohr, C.Fercher, K.Arends, R.Birner-Gruenberger, D.Laverde-Gomez, J.Huebner, E.Grohmann, W.Keller.
 
  ABSTRACT  
 
Conjugative plasmid transfer presents a serious threat to human health as the most important means of spreading antibiotic resistance and virulence genes among bacteria. The required direct cell-cell contact is established by a multi-protein complex, the conjugative type IV secretion system (T4SS). The conjugative core complex spans the cellular envelope and serves as a channel for macromolecular secretion. T4SSs of Gram-negative (G-) origin have been studied in great detail. In contrast, T4SSs of Gram-positive (G+) bacteria have only received little attention thus far, despite the medical relevance of numerous G+ pathogens (e.g. enterococci, staphylococci and streptococci). This study provides structural information on the type IV secretion (T4S) protein TraK of the G+ broad host range Enterococcus conjugative plasmid pIP501. The crystal structure of the N-terminally truncated construct TraKΔ was determined to 3.0 Å resolution and exhibits a novel fold. Immunolocalization demonstrated that the protein localizes to the cell wall facing towards the cell exterior, but does not exhibit surface accessibility. Circular dichroism, dynamic light scattering and size-exclusion chromatography confirmed the protein to be a monomer. With the exception of proteins from closely related T4SSs, no significant sequence or structural relatives were found. This observation marks the protein as a very exclusive, specialized member of the pIP501 T4SS.
 

 

spacer

spacer