› 4mva

X-ray diffraction
1.43Å resolution

1.43 Angstrom Resolution Crystal Structure of Triosephosphate Isomerase (tpiA) from Escherichia coli in Complex with Acetyl Phosphate.

Released:
DOI: 10.2210/pdb4mva/pdb
PDB entry 4mva coloured by chain, front view.
PDB entry 4mva coloured by chain, side view.
PDB entry 4mva coloured by chain, top view.
Source organism: Escherichia coli BW2952
Primary publication:
Structural, kinetic and proteomic characterization of acetyl phosphate-dependent bacterial protein acetylation.
Kuhn ML, Zemaitaitis B, Hu LI, Sahu A, Sorensen D, Minasov G, Lima BP, Scholle M, Mrksich M, Anderson WF, Gibson BW, Schilling B, Wolfe AJ
PLoS One 9 e94816 (2014)
PMID: 24756028

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-164845 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Triosephosphate isomerase Chains: A, B
Molecule details ›
Chains: A, B
Length: 279 amino acids
Theoretical weight: 29.75 KDa
Source organism: Escherichia coli BW2952
Expression system: Escherichia coli
Structure domains: Aldolase class I

Ligands and Environments

5 bound ligands:
Ligand CL 1 x CL
Ligand UVW 2 x UVW
Ligand PO4 1 x PO4
Ligand EDO 2 x EDO
Ligand PEG 1 x PEG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-G
Spacegroup: P212121
Unit cell:
a: 46.535Å b: 67.529Å c: 150.336Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.136 0.135 0.156
Expression system: Escherichia coli

Quick links

Citations

25 review citations

Acetyl coenzyme A: a central metabolite and second messenger.
Pietrocola et al. (2015)
24 more

1 mention without citation

Structural, kinetic and proteomic characterization of acetyl phosphate-dependent bacterial protein acetylation.
Kuhn et al. (2014)