› 2ozt

X-ray diffraction
1.42Å resolution

Crystal structure of O-succinylbenzoate synthase from Thermosynechococcus elongatus BP-1

Released:
DOI: 10.2210/pdb2ozt/pdb
PDB entry 2ozt coloured by chain, front view.
PDB entry 2ozt coloured by chain, side view.
PDB entry 2ozt coloured by chain, top view.
Source organism: Synechococcus elongatus
Primary publication:
Loss of quaternary structure is associated with rapid sequence divergence in the OSBS family.
Odokonyero D, Sakai A, Patskovsky Y, Malashkevich VN, Fedorov AA, Bonanno JB, Fedorov EV, Toro R, Agarwal R, Wang C, Ozerova ND, Yew WS, Sauder JM, Swaminathan S, Burley SK, Almo SC, Glasner ME
Proc Natl Acad Sci U S A 111 8535-40 (2014)
PMID: 24872444

Function and Biology Details

Reaction catalysed: 
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate = 2-succinylbenzoate + H(2)O
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-184081 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
o-succinylbenzoate synthase Chain: A
Molecule details ›
Chain: A
Length: 332 amino acids
Theoretical weight: 37.62 KDa
Source organism: Synechococcus elongatus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8DJP8 (Residues: 2-322; Coverage: 100%)
Gene names: menC, tlr1174
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand PO4 2 x PO4
Ligand NA 1 x NA
1 modified residue:
Ligand MSE 3 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 31-ID
Spacegroup: C2221
Unit cell:
a: 39.641Å b: 113.498Å c: 148.155Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.179 0.178 0.207
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

Biosynthesis and applications of prenylquinones.
Kawamukai M. (2018)
2 more

2 mentions without citation

Dead-end elimination with perturbations (DEEPer): a provable protein design algorithm with continuous sidechain and backbone flexibility.
Hallen et al. (2013)
1 more