› 2lfv

Solution NMR

Solution Structure of the SPOR domain from E. coli DamX

Released:
DOI: 10.2210/pdb2lfv/pdb
PDB entry 2lfv coloured by chain, ensemble of 25 models, front view.
PDB entry 2lfv coloured by chain, ensemble of 25 models, side view.
PDB entry 2lfv coloured by chain, ensemble of 25 models, top view.
Source organism: Escherichia coli K-12
Primary publication:
Nuclear magnetic resonance solution structure of the peptidoglycan-binding SPOR domain from Escherichia coli DamX: insights into septal localization.
Williams KB, Yahashiri A, Arends SJ, Popham DL, Fowler CA, Weiss DS
Biochemistry 52 627-39 (2013)
PMID: 23290046

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145875 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cell division protein DamX Chain: A
Molecule details ›
Chain: A
Length: 106 amino acids
Theoretical weight: 11.88 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P11557 (Residues: 338-428; Coverage: 21%)
Gene names: JW3351, b3388, damX, yhfB
Sequence domains: SPOR domain
Structure domains: Sporulation related repeat

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 96%
Refinement method: torsion angle dynamics
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Regulation of bacterial cell wall growth.
Egan et al. (2017)
1 more

3 mentions without citation

Identification of SPOR domain amino acids important for septal localization, peptidoglycan binding, and a disulfide bond in the cell division protein FtsN.
Duncan et al. (2013)
2 more