› 4y68

X-ray diffraction
2.21Å resolution

Structure of a lipoprotein from Streptococcus agalactiae

Released:
DOI: 10.2210/pdb4y68/pdb
PDB 4y68 coloured by chain and viewed from the front.
PDB 4y68 coloured by chain and viewed from the side.
PDB 4y68 coloured by chain and viewed from the top.
Source organism: Streptococcus agalactiae 515
Primary publication:
Structural basis of lantibiotic recognition by the nisin resistance protein from Streptococcus agalactiae.
Khosa S, Frieg B, Mulnaes D, Kleinschrodt D, Hoeppner A, Gohlke H, Smits SH
Sci Rep 6 18679 (2016)
PMID: 26727488

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tail specific protease domain-containing protein Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 312 amino acids
Theoretical weight: 35.46 KDa
Source organism: Streptococcus agalactiae 515
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0A140UHB6 (Residues: 1-167; Coverage: 100%)
Gene name: SAL_1042
Sequence domains: Peptidase family S41

Ligands and Environments

1 bound ligand:
Ligand MES 4 x MES
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-2
Spacegroup: P212121
Unit cell:
a: 58.81Å b: 137.24Å c: 164Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.196 0.194 0.243
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

8 review citations

Nisin Variants Generated by Protein Engineering and Their Properties.
Zheng et al. (2022)
7 more

3 mentions without citation

Mechanistic Understanding of Lanthipeptide Biosynthetic Enzymes.
Repka et al. (2017)
2 more