PDBsum entry 5n2c

Transport protein

PDB id: 5n2c

Contents

Protein chains

119 a.a.

Ligands

EDO ×5

CXS ×3

OXL ×3

ACT ×4

Waters ×189

PDB id:

5n2c

Name:

Transport protein

Title:

Crystal structure of the peptidoglycan-associated lipoprotein from burkholderia cenocepacia

Structure:

Putative ompa family lipoprotein. Chain: a, b, c. Engineered: yes. Other_details: the signal peptide was removed

Source:

Burkholderia cenocepacia j2315. Organism_taxid: 216591. Gene: bcal3204. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Expression_system_variant: star.

Resolution:

1.80Å R-factor: 0.180 R-free: 0.219

Authors:

E.Matterazzo,M.Bolognesi,L.J.Gourlay

Key ref:

R.Capelli et al. (2017). Designing Probes for Immunodiagnostics: Structural Insights into an Epitope Targeting Burkholderia Infections. ACS Infect Dis, 3, 736-743. PubMed id: 28707874 DOI: 10.1021/acsinfecdis.7b00080

Date:

07-Feb-17 Release date: 26-Jul-17

Protein chains

B4EDC1  (B4EDC1_BURCJ) -  Peptidoglycan-associated lipoprotein from Burkholderia cenocepacia (strain ATCC BAA-245 / DSM 16553 / LMG 16656 / NCTC 13227 / J2315 / CF5610)

Seq: 170 a.a.

Struc: 119 a.a.

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1021/acsinfecdis.7b00080

ACS Infect Dis 3:736-743 (2017)

PubMed id: 28707874

Designing Probes for Immunodiagnostics: Structural Insights into an Epitope Targeting Burkholderia Infections.

R.Capelli, E.Matterazzo, M.Amabili, C.Peri, A.Gori, P.Gagni, M.Chiari, G.Lertmemongkolchai, M.Cretich, M.Bolognesi, G.Colombo, L.J.Gourlay.

ABSTRACT

Structure-based epitope prediction drives the design of diagnostic peptidic probes to reveal specific antibodies elicited in response to infections. We previously identified a highly immunoreactive epitope from the peptidoglycan-associated lipoprotein (Pal) antigen from Burkholderia pseudomallei, which could also diagnose Burkholderia cepacia infections. Here, considering the high phylogenetic conservation within Burkholderia species, we ask whether cross-reactivity can be reciprocally displayed by the synthetic epitope from B. cenocepacia. We perform comparative analyses of the conformational preferences and diagnostic performances of the corresponding epitopes from the two Burkholderia species when presented in the context of the full-length proteins or as isolated peptides. The effects of conformation on the diagnostic potential and cross-reactivity of Pal peptide epitopes are rationalized on the basis of the 1.8 Å crystal structure of B. cenocepacia Pal and through computational analyses. Our results are discussed in the context of designing new diagnostic molecules for the early detection of infectious diseases.