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PDBsum entry 4b5c

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protein ligands Protein-protein interface(s) links
Lipid transport PDB id
4b5c

 

 

 

 

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Contents
Protein chains
119 a.a.
Ligands
ACT ×3
Waters ×60
PDB id:
4b5c
Name: Lipid transport
Title: Crystal structure of the peptidoglycan-associated lipoprotein from burkholderia pseudomallei
Structure: Putative ompa family lipoprotein. Chain: a, b, c. Fragment: residues 36-170. Synonym: peptidoglycan-associated lipoprotein. Engineered: yes
Source: Burkholderia pseudomallei. Organism_taxid: 28450. Strain: k96423. Expressed in: escherichia coli. Expression_system_taxid: 469008. Expression_system_variant: star.
Resolution:
2.30Å     R-factor:   0.209     R-free:   0.249
Authors: L.J.Gourlay,C.Peri,O.Conchillo-Sole,M.Ferrer-Navarro,A.Gori,R.Longhi, D.Rinchai,G.Lertmemongkolchai,P.Lassaux,X.Daura,G.Colombo, M.Bolognesi
Key ref: L.J.Gourlay et al. (2013). Exploiting the Burkholderia pseudomallei acute phase antigen BPSL2765 for structure-based epitope discovery/design in structural vaccinology. Chem Biol, 20, 1147-1156. PubMed id: 23993463 DOI: 10.1016/j.chembiol.2013.07.010
Date:
03-Aug-12     Release date:   14-Aug-13    
PROCHECK
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 Headers
 References

Protein chains
Q63RA7  (Q63RA7_BURPS) -  Peptidoglycan-associated lipoprotein from Burkholderia pseudomallei (strain K96243)
Seq:
Struc:
170 a.a.
119 a.a.
Key:    Secondary structure  CATH domain

 

 
DOI no: 10.1016/j.chembiol.2013.07.010 Chem Biol 20:1147-1156 (2013)
PubMed id: 23993463  
 
 
Exploiting the Burkholderia pseudomallei acute phase antigen BPSL2765 for structure-based epitope discovery/design in structural vaccinology.
L.J.Gourlay, C.Peri, M.Ferrer-Navarro, O.Conchillo-Solé, A.Gori, D.Rinchai, R.J.Thomas, O.L.Champion, S.L.Michell, C.Kewcharoenwong, A.Nithichanon, P.Lassaux, L.Perletti, R.Longhi, G.Lertmemongkolchai, R.W.Titball, X.Daura, G.Colombo, M.Bolognesi.
 
  ABSTRACT  
 
We solved the crystal structure of Burkholderia pseudomallei acute phase antigen BPSL2765 in the context of a structural vaccinology study, in the area of melioidosis vaccine development. Based on the structure, we applied a recently developed method for epitope design that combines computational epitope predictions with in vitro mapping experiments and successfully identified a consensus sequence within the antigen that, when engineered as a synthetic peptide, was selectively immunorecognized to the same extent as the recombinant protein in sera from melioidosis-affected subjects. Antibodies raised against the consensus peptide were successfully tested in opsonization bacterial killing experiments and antibody-dependent agglutination tests of B. pseudomallei. Our strategy represents a step in the development of immunodiagnostics, in the production of specific antibodies and in the optimization of antigens for vaccine development, starting from structural and physicochemical principles.
 

 

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