› 3hpi

X-ray diffraction
2Å resolution

Crystal structure of maltose-binding protein mutant with bound sucrose

Released:
DOI: 10.2210/pdb3hpi/pdb
PDB entry 3hpi coloured by chain, front view.
PDB entry 3hpi coloured by chain, side view.
PDB entry 3hpi coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Studies of the maltose transport system reveal a mechanism for coupling ATP hydrolysis to substrate translocation without direct recognition of substrate.
Gould AD, Shilton BH
J Biol Chem 285 11290-6 (2010)
PMID: 20147285

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142613 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Maltose/maltodextrin-binding periplasmic protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 372 amino acids
Theoretical weight: 40.91 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P0AEX9 (Residues: 27-396; Coverage: 100%)
Gene names: JW3994, b4034, malE
Sequence domains: Bacterial extracellular solute-binding protein
Structure domains: Periplasmic binding protein-like II

Ligands and Environments

Carbohydrate polymer : NEW Components: GLC, FRU
Carbohydrate polymer
2 bound ligands:
Ligand ZN 6 x ZN
Ligand ACT 2 x ACT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CLSI BEAMLINE 08ID-1
Spacegroup: P212121
Unit cell:
a: 60.042Å b: 85.229Å c: 132.864Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.241 0.228 0.284
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Canonical and ECF-type ATP-binding cassette importers in prokaryotes: diversity in modular organization and cellular functions.
Eitinger et al. (2011)
4 more

8 mentions without citation

Therapeutic Bacteriophages for Gram-Negative Bacterial Infections in Animals and Humans.
Zagaliotis et al. (2022)
7 more