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X-ray diffraction
1.85Å resolution

CRYSTAL STRUCTURE OF MALE31, A DEFECTIVE FOLDING MUTANT OF MALTOSE-BINDING PROTEIN

Released:
DOI: 10.2210/pdb1lax/pdb
PDB entry 1lax coloured by chain, front view.
PDB entry 1lax coloured by chain, side view.
PDB entry 1lax coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Crystal structure of a defective folding protein.
Saul FA, Mourez M, Vulliez-Le Normand B, Sassoon N, Bentley GA, Betton JM
Protein Sci 12 577-85 (2003)
PMID: 12592028

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 Chains: A, C
Molecule details ›
Chains: A, C
Length: 370 amino acids
Theoretical weight: 40.8 KDa
Source organism: Escherichia coli
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
X-ray source: ESRF BEAMLINE ID14-3
Spacegroup: P21
Unit cell:
a: 42.043Å b: 89.115Å c: 95.975Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.159 0.157 0.202
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Interactions between folding factors and bacterial outer membrane proteins.
Mogensen et al. (2005)
1 more

2 mentions without citation

Catalytically-active inclusion bodies for biotechnology-general concepts, optimization, and application.
Jäger et al. (2020)
1 more