› 1usi

X-ray diffraction
1.8Å resolution

L-leucine-binding protein with phenylalanine bound

Released:
DOI: 10.2210/pdb1usi/pdb
PDB 1usi coloured by chain and viewed from the front.
PDB 1usi coloured by chain and viewed from the side.
PDB 1usi coloured by chain and viewed from the top.
Source organism: Escherichia coli
Primary publication:
X-ray structures of the leucine-binding protein illustrate conformational changes and the basis of ligand specificity.
Magnusson U, Salopek-Sondi B, Luck LA, Mowbray SL
J. Biol. Chem. 279 8747-52 (2004)
PMID: 14672931

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Leucine-specific-binding protein Chains: A, C
Molecule details ›
Chains: A, C
Length: 346 amino acids
Theoretical weight: 37.08 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P04816 (Residues: 24-369; Coverage: 100%)
Gene names: JW3423, b3458, livK
Sequence domains: Periplasmic binding protein
Structure domains: Rossmann fold

Ligands and Environments

1 bound ligand:
Ligand PHE 2 x PHE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I711
Spacegroup: P21
Unit cell:
a: 68.236Å b: 78.143Å c: 70.183Å
α: 90° β: 102.82° γ: 90°
R-values:
R R work R free
0.191 0.189 0.222
Expression system: Escherichia coli BL21

Quick links

Citations

2 review citations

Selective substrate uptake: The role of ATP-binding cassette (ABC) importers in pathogenesis.
Tanaka et al. (2018)
1 more

6 mentions without citation

Coevolutionary signals across protein lineages help capture multiple protein conformations.
Morcos et al. (2013)
5 more