PDBsum entry 2mtc

Protein binding

PDB id: 2mtc

Contents

Protein chain

166 a.a.

PDB id:

2mtc

Name:

Protein binding

Title:

Structure of decorin binding protein a from strain n40 of borrelia burgdorferi

Structure:

Decorin-binding protein a. Chain: a. Fragment: unp residues 29-194. Engineered: yes

Source:

Borrelia burgdorferi. Organism_taxid: 521007. Strain: n40. Gene: bbun40_a24, dbp. Expressed in: escherichia coli. Expression_system_taxid: 469008.

NMR struc:

10 models

Authors:

X.Wang,A.Morgan

Key ref:

A.M.Morgan and X.Wang (2015). Structural mechanisms underlying sequence-dependent variations in GAG affinities of decorin binding protein A, a Borrelia burgdorferi adhesin. Biochem J, 467, 439-451. PubMed id: 25695518 DOI: 10.1042/BJ20141201

Date:

16-Aug-14 Release date: 25-Mar-15

Protein chain

A0A0J9X1X0  (A0A0J9X1X0_BORBN) -  Decorin-binding protein A from Borreliella burgdorferi (strain N40)

Seq: 166 a.a.

Struc: 166 a.a.

DOI no: 10.1042/BJ20141201

Biochem J 467:439-451 (2015)

PubMed id: 25695518

Structural mechanisms underlying sequence-dependent variations in GAG affinities of decorin binding protein A, a Borrelia burgdorferi adhesin.

A.M.Morgan, X.Wang.

ABSTRACT

Decorin-binding protein A (DBPA) is an important surface adhesin of the bacterium Borrelia burgdorferi, the causative agent of Lyme disease. DBPA facilitates the bacteria's colonization of human tissue by adhering to glycosaminoglycan (GAG), a sulfated polysaccharide. Interestingly, DBPA sequence variation among different strains of Borrelia spirochetes is high, resulting in significant differences in their GAG affinities. However, the structural mechanisms contributing to these differences are unknown. We determined the solution structures of DBPAs from strain N40 of B. burgdorferi and strain PBr of Borrelia garinii, two DBPA variants whose GAG affinities deviate significantly from strain B31, the best characterized version of DBPA. Our structures revealed that significant differences exist between PBr DBPA and B31/N40 DBPAs. In particular, the C-terminus of PBr DBPA, unlike C-termini from B31 and N40 DBPAs, is positioned away from the GAG-binding pocket and the linker between helices one and two of PBr DBPA is highly structured and retracted from the GAG-binding pocket. The repositioning of the C-terminus allowed the formation of an extra GAG-binding epitope in PBr DBPA and the retracted linker gave GAG ligands more access to the GAG-binding epitopes than other DBPAs. Characterization of GAG ligands' interactions with wild-type (WT) PBr and mutants confirmed the importance of the second major GAG-binding epitope and established the fact that the two epitopes are independent of one another and the new epitope is as important to GAG binding as the traditional epitope.