› 4eaa

X-ray diffraction
1.45Å resolution

X-ray crystal structure of the H141N mutant of perosamine N-acetyltransferase from Caulobacter crescentus in complex with CoA and GDP-perosamine

Released:
DOI: 10.2210/pdb4eaa/pdb
PDB entry 4eaa coloured by chain, front view.
PDB entry 4eaa coloured by chain, side view.
PDB entry 4eaa coloured by chain, top view.
Source organism: Caulobacter vibrioides
Primary publication:
Catalytic mechanism of perosamine N-acetyltransferase revealed by high-resolution X-ray crystallographic studies and kinetic analyses.
Thoden JB, Reinhardt LA, Cook PD, Menden P, Cleland WW, Holden HM
Biochemistry 51 3433-44 (2012)
PMID: 22443398

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-131435 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
PglD N-terminal domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 220 amino acids
Theoretical weight: 21.89 KDa
Source organism: Caulobacter vibrioides
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O85353 (Residues: 2-215; Coverage: 100%)
Gene name: wbqR
Sequence domains: PglD N-terminal domain
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand JB2 1 x JB2
Ligand COA 1 x COA
Ligand NA 1 x NA
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: I23
Unit cell:
a: 115.007Å b: 115.007Å c: 115.007Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.181 0.18 0.21
Expression system: Escherichia coli BL21(DE3)

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Citations

14 citation in other articles

Structure of soybean serine acetyltransferase and formation of the cysteine regulatory complex as a molecular chaperone.
Yi et al. (2013)
13 more

1 mention without citation

Catalytic mechanism of perosamine N-acetyltransferase revealed by high-resolution X-ray crystallographic studies and kinetic analyses.
Thoden et al. (2012)