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Crystal structure of outer membrane lipoprotein carrier protein (LolA) from Borrelia burgdorferi (steric acid bound)

X-ray diffraction
1.8Å resolution
PDB entry 8t5t coloured by chain, front view.
PDB entry 8t5t coloured by chain, side view.
PDB entry 8t5t coloured by chain, top view.
Source organism: Borreliella burgdorferi B31
Assembly composition:
monomeric (preferred)
Entry contents: 1 distinct polypeptide molecule

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Assemblies

Assembly 1 (preferred)
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Assembly Name: Export chaperone
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Multimeric state: monomeric
Accessible surface area: 9835.03 Å2
Buried surface area: 2262.42 Å2
Dissociation area: 449.88 Å2
Dissociation energy (ΔGdiss): -4.13 kcal/mol
Dissociation entropy (TΔSdiss): 4.21 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-129353

Macromolecules

Export chaperone
Chain: A
Length: 208 amino acids
Theoretical weight: 23.4 KDa
Source organism: Borreliella burgdorferi B31
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O51321 (Residues: 18-216; Coverage: 92%)
Gene name: BB_0346
Pfam: Outer membrane lipoprotein carrier protein LolA
Export chaperone in PDB entry 8t5t, assembly 1, front view.
Export chaperone in PDB entry 8t5t, assembly 1, side view.
Export chaperone in PDB entry 8t5t, assembly 1, top view.
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