2LQU

Structure of decorbin-binding protein A from Borrelia burgdorferi

Summary for 2LQU

• Entry DOI: 10.2210/pdb2lqu/pdb
• NMR Information: BMRB: 18329
• Descriptor: Decorin-binding protein A (1 entity in total)
• Functional Keywords: gag-binding protein, helical bundle protein, lyme disease, bacterial adhesin, cell adhesion
• Biological source: Borrelia burgdorferi (Lyme disease spirochete)
• Total number of polymer chains: 1
• Total formula weight: 18555.18

Authors

Wang, X. (deposition date: 2012-03-14, release date: 2013-01-16, Last modification date: 2024-11-20)

Primary citation

Wang, X.
Solution structure of decorin-binding protein A from Borrelia burgdorferi.
Biochemistry, 51:8353-8362, 2012

PubMed Abstract: Decorin-binding protein A (DBPA) is an important lipoprotein from the bacterium Borrelia burgdorferi, the causative agent of Lyme disease. The absence of DBPA drastically reduces the pathogenic potential of the bacterium, and biochemical evidence indicates DBPA's interactions with the glycosaminoglycan (GAG) portion of decorin are crucial to its function. We have determined the solution structure of DBPA and studied DBPA's interactions with various forms of GAGs. DBPA is determined to be a helical bundle protein consisting of five helices held together by a strong hydrophobic core. The structure also possesses a basic patch formed by portions of two helices and two flexible linkers. Low-molecular mass heparin-induced chemical shift perturbations for residues in the region as well as increases in signal intensities of select residues in their presence confirm residues in the pocket are perturbed by heparin binding. Dermatan sulfate fragments, the dominant GAG type found on decorin, were shown to have lower affinity than heparin but are still capable of binding DBPA.

PubMed: 22985470
DOI: 10.1021/bi3007093

Experimental method

SOLUTION NMR