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5N2C

Crystal structure of the peptidoglycan-associated lipoprotein from Burkholderia cenocepacia

Summary for 5N2C
Entry DOI10.2210/pdb5n2c/pdb
DescriptorPutative OmpA family lipoprotein, 1,2-ETHANEDIOL, 3-CYCLOHEXYL-1-PROPYLSULFONIC ACID, ... (6 entities in total)
Functional Keywordsouter membrane protein a like domain, lipoprotein, antigen, transport protein
Biological sourceBurkholderia cenocepacia J2315
Total number of polymer chains3
Total formula weight63177.74
Authors
Matterazzo, E.,Bolognesi, M.,Gourlay, L.J. (deposition date: 2017-02-07, release date: 2017-07-26, Last modification date: 2024-01-17)
Primary citationCapelli, R.,Matterazzo, E.,Amabili, M.,Peri, C.,Gori, A.,Gagni, P.,Chiari, M.,Lertmemongkolchai, G.,Cretich, M.,Bolognesi, M.,Colombo, G.,Gourlay, L.J.
Designing Probes for Immunodiagnostics: Structural Insights into an Epitope Targeting Burkholderia Infections.
ACS Infect Dis, 3:736-743, 2017
Cited by
PubMed 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.
PubMed: 28707874
DOI: 10.1021/acsinfecdis.7b00080
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.8 Å)
Structure validation

237735

數據於2025-06-18公開中

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