› 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 entry 4oko coloured by chain, front view.
PDB entry 4oko coloured by chain, side view.
PDB entry 4oko coloured by chain, top view.
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 289 30668-30679 (2014)
PMID: 25231992

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-106175 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Rapid Encystment Phenotype Protein 34 KDa 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 name: 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