› 1omp

X-ray diffraction
1.8Å resolution

CRYSTALLOGRAPHIC EVIDENCE OF A LARGE LIGAND-INDUCED HINGE-TWIST MOTION BETWEEN THE TWO DOMAINS OF THE MALTODEXTRIN-BINDING PROTEIN INVOLVED IN ACTIVE TRANSPORT AND CHEMOTAXIS

Released:
DOI: 10.2210/pdb1omp/pdb
PDB entry 1omp coloured by chain, front view.
PDB entry 1omp coloured by chain, side view.
PDB entry 1omp coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Crystallographic evidence of a large ligand-induced hinge-twist motion between the two domains of the maltodextrin binding protein involved in active transport and chemotaxis.
Sharff AJ, Rodseth LE, Spurlino JC, Quiocho FA
Biochemistry 31 10657-63 (1992)
PMID: 1420181

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: 40.75 KDa
Source organism: Escherichia coli
Expression system: Not provided
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: P1
Unit cell:
a: 38.35Å b: 44.44Å c: 58.25Å
α: 101° β: 100.4° γ: 104.2°
R-values:
R R work R free
0.21 0.21 not available
Expression system: Not provided

Quick links

Citations

47 review citations

Extracellular calcium sensing and extracellular calcium signaling.
Brown et al. (2001)
46 more

98 mentions without citation

Global dynamics of proteins: bridging between structure and function.
Bahar et al. (2010)
97 more