› 1mpd

X-ray diffraction
2.3Å resolution

MALTODEXTRIN-BINDING PROTEIN (MALTOSE-BINDING PROTEIN) MUTANT, WITH ARGININE REPLACING TRYPTOPHAN AT POSITION 230 (TRP-230-ARG), COMPLEXED WITH MALTOSE

Released:
DOI: 10.2210/pdb1mpd/pdb
PDB entry 1mpd coloured by chain, front view.
PDB entry 1mpd coloured by chain, side view.
PDB entry 1mpd coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Crystal structures and solution conformations of a dominant-negative mutant of Escherichia coli maltose-binding protein.
Shilton BH, Shuman HA, Mowbray SL
J Mol Biol 264 364-76 (1996)
PMID: 8951382

Function and Biology Details

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

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 Chain: A
Molecule details ›
Chain: A
Length: 370 amino acids
Theoretical weight: 40.72 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
Carbohydrate polymer
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 53.68Å b: 58.96Å c: 126.92Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.168 0.168 not available
Expression system: Escherichia coli

Quick links

Citations

7 review citations

Maltose/maltodextrin system of Escherichia coli: transport, metabolism, and regulation.
Boos et al. (1998)
6 more

3 mentions without citation

Decoding the chemotactic signal.
Thomas et al. (2018)
2 more