› 1mpb

X-ray diffraction
2Å resolution

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

Released:
DOI: 10.2210/pdb1mpb/pdb
PDB entry 1mpb coloured by chain, front view.
PDB entry 1mpb coloured by chain, side view.
PDB entry 1mpb 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
Macromolecule:
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

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 44.52Å b: 82.89Å c: 58.22Å
α: 90° β: 101.57° γ: 90°
R-values:
R R work R free
0.182 0.182 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

2 mentions without citation

Major Impacts of Widespread Structural Variation on Gene Expression and Crop Improvement in Tomato.
Alonge et al. (2020)
1 more