› 4oko

X-ray diffraction
2.05Å resolution

Crystal structure of Francisella tularensis REP34 (Rapid Encystment Phenotype Protein 34 KDa)

Released:
DOI: 10.2210/pdb4oko/pdb
PDB 4oko coloured by chain and viewed from the front.
PDB 4oko coloured by chain and viewed from the side.
PDB 4oko coloured by chain and viewed from the top.
Source organism: Francisella tularensis subsp. novicida U112
Primary publication:
Structure and function of REP34 implicates carboxypeptidase activity in Francisella tularensis host-cell invasion.
Feld GK, El-Etr S, Corzett MH, Hunter MS, Belhocine K, Monack DM, Frank M, Segelke BW, Rasley A
J. Biol. Chem. (2014)
PMID: 25231992

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidase_M14 domain-containing protein Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 312 amino acids
Theoretical weight: 35.38 KDa
Source organism: Francisella tularensis subsp. novicida U112
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0Q494 (Residues: 1-304; Coverage: 100%)
Gene names: AW25_51, FTN_0149
Sequence domains: Zinc carboxypeptidase
Structure domains: Zn peptidases

Ligands and Environments

2 bound ligands:
Ligand ZN 4 x ZN
Ligand ACT 4 x ACT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-D
Spacegroup: P1
Unit cell:
a: 62.712Å b: 63.308Å c: 81.689Å
α: 70.36° β: 84.34° γ: 82.53°
R-values:
R R work R free
0.213 0.213 0.232
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 citations in other articles

Functional Annotation from Structural Homology.
Segelke BW. (2022)

2 mentions without citation

Self-association of a highly charged arginine-rich cell-penetrating peptide.
Tesei et al. (2017)
1 more