› 3tre

X-ray diffraction
2.9Å resolution

Structure of a translation elongation factor P (efp) from Coxiella burnetii

Released:
DOI: 10.2210/pdb3tre/pdb
PDB entry 3tre coloured by chain, front view.
PDB entry 3tre coloured by chain, side view.
PDB entry 3tre coloured by chain, top view.
Source organism: Coxiella burnetii
Primary publication:
Structural genomics for drug design against the pathogen Coxiella burnetii.
Franklin MC, Cheung J, Rudolph MJ, Burshteyn F, Cassidy M, Gary E, Hillerich B, Yao ZK, Carlier PR, Totrov M, Love JD
Proteins 83 2124-36 (2015)
PMID: 26033498

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-182899 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Elongation factor P Chain: A
Molecule details ›
Chain: A
Length: 191 amino acids
Theoretical weight: 21.63 KDa
Source organism: Coxiella burnetii
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q83AR4 (Residues: 1-188; Coverage: 100%)
Gene names: CBU_1816, efp
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 6 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P63
Unit cell:
a: 82.619Å b: 82.619Å c: 79.096Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.237 0.235 0.271
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

5 review citations

Laccases of prokaryotic origin: enzymes at the interface of protein science and protein technology.
Martins et al. (2015)
4 more

1 mention without citation

Single-residue posttranslational modification sites at the N-terminus, C-terminus or in-between: To be or not to be exposed for enzyme access.
Sirota et al. (2015)