› 1pv6

X-ray diffraction
3.5Å resolution

Crystal structure of lactose permease

Released:
DOI: 10.2210/pdb1pv6/pdb
PDB entry 1pv6 coloured by chain, front view.
PDB entry 1pv6 coloured by chain, side view.
PDB entry 1pv6 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structure and mechanism of the lactose permease of Escherichia coli.
Abramson J, Smirnova I, Kasho V, Verner G, Kaback HR, Iwata S
Science 301 610-5 (2003)
PMID: 12893935

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:
Lactose permease Chains: A, B
Molecule details ›
Chains: A, B
Length: 417 amino acids
Theoretical weight: 46.48 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P02920 (Residues: 1-417; Coverage: 100%)
Gene names: JW0334, b0343, lacY
Sequence domains: LacY proton/sugar symporter
Structure domains: MFS general substrate transporter like domains

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P212121
Unit cell:
a: 101.351Å b: 125.845Å c: 188.118Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.294 0.294 0.337
Expression system: Escherichia coli

Quick links

Citations

207 review citations

How phosphotransferase system-related protein phosphorylation regulates carbohydrate metabolism in bacteria.
Deutscher et al. (2006)
206 more

53 mentions without citation

The alternating access transport mechanism in LacY.
Kaback et al. (2011)
52 more