› 4y68

X-ray diffraction
2.21Å resolution

Structure of a lipoprotein from Streptococcus agalactiae

Released:
DOI: 10.2210/pdb4y68/pdb
PDB entry 4y68 coloured by chain, front view.
PDB entry 4y68 coloured by chain, side view.
PDB entry 4y68 coloured by chain, top view.
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:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-102988 (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

13 review citations

Employing the promiscuity of lantibiotic biosynthetic machineries to produce novel antimicrobials.
Montalbán-López et al. (2017)
12 more

3 mentions without citation

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