› 1r48

Solution NMR

Solution structure of the C-terminal cytoplasmic domain residues 468-497 of Escherichia coli protein ProP

Released:
DOI: 10.2210/pdb1r48/pdb
PDB 1r48 coloured by chain and viewed from the front.
PDB 1r48 coloured by chain and viewed from the side.
PDB 1r48 coloured by chain and viewed from the top.
Source organism: Escherichia coli
Primary publication:
Solution structure of the C-terminal antiparallel coiled-coil domain from Escherichia coli osmosensor ProP.
Zoetewey DL, Tripet BP, Kutateladze TG, Overduin MJ, Wood JM, Hodges RS
J. Mol. Biol. 334 1063-76 (2003)
PMID: 14643666

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Proline/betaine transporter Chains: A, B
Molecule details ›
Chains: A, B
Length: 33 amino acids
Theoretical weight: 3.82 KDa
Source organism: Escherichia coli
Expression system: Not provided
UniProt:
  • Canonical: P0C0L7 (Residues: 468-497; Coverage: 6%)
Gene names: JW4072, b4111, proP

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing
Chemical shifts: BMR5972  
Expression system: Not provided

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Citations

3 review citations

Bacterial osmoregulation: a paradigm for the study of cellular homeostasis.
Wood JM. (2011)
2 more

6 mentions without citation

Bacterial responses to osmotic challenges.
Wood JM. (2015)
5 more