› 6qbi

Solution NMR

NMR structure of BB_P28, Borrelia burgdorferi outer surface lipoprotein

Released:
DOI: 10.2210/pdb6qbi/pdb
PDB entry 6qbi coloured by chain, ensemble of 20 models, front view.
PDB entry 6qbi coloured by chain, ensemble of 20 models, side view.
PDB entry 6qbi coloured by chain, ensemble of 20 models, top view.
Source organism: Borreliella burgdorferi B31
Primary publication:
Solution NMR structure of Borrelia burgdorferi outer surface lipoprotein BBP28, a member of the mlp protein family.
Fridmanis J, Otikovs M, Brangulis K, Tārs K, Jaudzems K
Proteins 89 588-594 (2021)
PMID: 32949018

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-124880 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lipoprotein MlpA Chain: A
Molecule details ›
Chain: A
Length: 102 amino acids
Theoretical weight: 11.04 KDa
Source organism: Borreliella burgdorferi B31
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: H7C7P1 (Residues: 51-148; Coverage: 75%)
Gene names: BB_P28, mlpA
Sequence domains: Mlp lipoprotein family

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this NMR entry.
Chemical shift assignment: 96%
Refinement method: torsion angle dynamics
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Erp and Rev Adhesins of the Lyme Disease Spirochete's Ubiquitous cp32 Prophages Assist the Bacterium during Vertebrate Infection.
Stevenson et al. (2023)

1 mention without citation

Structural and Functional Analysis of BBA03, Borrelia burgdorferi Competitive Advantage Promoting Outer Surface Lipoprotein.
Fridmanis et al. (2020)