7S0R: C protein beta antigen

Crystal Structure of a Complement Factor H-binding Fragment within the B75KN Region of the Group B Streptococcus Beta Antigen C Protein. Determined by X-ray diffraction at 2.5 Å resolution. Released 15 Dec 2021.

Method: X-ray diffraction
Resolution: 2.5 Å
Organism: Streptococcus agalactiae
Chains: 2
Atoms: 1,320
Mol. weight: 24.19 kDa
Released: 15 Dec 2021

Explore 7S0R in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7S0R contains 6 α-helices and 0 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 3 helices, 0 β-strands

Element	Residues	Length
α-helix	737-758	22
α-helix	775-792	18
α-helix	797-821	25

Chain B: 3 helices, 0 β-strands

Element	Residues	Length
α-helix	739-758	20
α-helix	773-792	20
α-helix	797-820	24

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
C protein beta antigen	A, B	protein	107	Streptococcus agalactiae	P27951 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>7S0R_1 C protein beta antigen (chains A, B)
GSTGSVEQDQPAPIPENSEMDQAKEKAKIAVSKYMSKVLDGVHQHLQKKNHSKIVDLFKE
LEAIKQQTIFDIDNAKTEVEIDNLVHDAFSKMNATVAKFQKGLETNT

Primary citation

Group B Streptococcus Surface Protein beta : Structural Characterization of a Complement Factor H-Binding Motif and Its Contribution to Immune Evasion. Xu, X., Lewis Marffy, A.L., Keightley, A. et al. J Immunol (2022) 208:1232-1247. DOI 10.4049/jimmunol.2101078 · PubMed

Other PDB entries of the same protein (UniProt P27951 (AlphaFold model), which also has an AlphaFold model), best resolution first:

9MN2 2.05 Å, Crystal Structure of the B6C Region of the Group B Streptococcus Beta Antigen C Protein
6V3P 3.25 Å, The BIgI domain of beta protein from S. agalactiae bound to CEACAM1
5WAH Solution NMR structure of siglec-5 binding domain from streptococcal beta protein

Browse structure collections

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