› 1fip

X-ray diffraction
1.9Å resolution

THE STRUCTURE OF FIS MUTANT PRO61ALA ILLUSTRATES THAT THE KINK WITHIN THE LONG ALPHA-HELIX IS NOT DUE TO THE PRESENCE OF THE PROLINE RESIDUE

Released:
DOI: 10.2210/pdb1fip/pdb
PDB entry 1fip coloured by chain, front view.
PDB entry 1fip coloured by chain, side view.
PDB entry 1fip coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
The structure of Fis mutant Pro61Ala illustrates that the kink within the long alpha-helix is not due to the presence of the proline residue.
Yuan HS, Wang SS, Yang WZ, Finkel SE, Johnson RC
J Biol Chem 269 28947-54 (1994)
PMID: 7961857

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141420 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
DNA-binding protein Fis Chains: A, B
Molecule details ›
Chains: A, B
Length: 98 amino acids
Theoretical weight: 11.23 KDa
Source organism: Escherichia coli
Expression system: Not provided
UniProt:
  • Canonical: P0A6R3 (Residues: 1-98; Coverage: 100%)
Gene names: JW3229, b3261, fis
Sequence domains: Bacterial regulatory protein, Fis family
Structure domains: Homeodomain-like
UNKNOWN PEPTIDE, POSSIBLY PART OF THE UNOBSERVED RESIDUES IN ENTITY 1 Chains: C, D
Molecule details ›
Chains: C, D
Length: 4 amino acids
Theoretical weight: 358 Da
Source organism: Escherichia coli
Expression system: Not provided

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 79.08Å b: 51.12Å c: 47.29Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.199 0.199 not available
Expression system: Not provided

Quick links

Citations

1 review citation

Location and nature of the residues important for ligand recognition in G-protein coupled receptors.
Bywater RP. (2005)
13 other articles

4 mentions without citation

Towards accurate residue-residue hydrophobic contact prediction for alpha helical proteins via integer linear optimization.
Rajgaria et al. (2009)
3 more