› 2v93

Solution NMR

EQUILLIBRIUM MIXTURE OF OPEN AND PARTIALLY-CLOSED SPECIES IN THE APO STATE OF MALTODEXTRIN-BINDING PROTEIN BY PARAMAGNETIC RELAXATION ENHANCEMENT NMR

Released:
DOI: 10.2210/pdb2v93/pdb
PDB entry 2v93 coloured by chain, ensemble of 50 models, front view.
PDB entry 2v93 coloured by chain, ensemble of 50 models, side view.
PDB entry 2v93 coloured by chain, ensemble of 50 models, top view.
Source organism: Escherichia coli
Primary publication:
Open-to-closed transition in apo maltose-binding protein observed by paramagnetic NMR.
Tang C, Schwieters CD, Clore GM
Nature 449 1078-82 (2007)
PMID: 17960247

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
Macromolecule:
Maltose/maltodextrin-binding periplasmic protein Chain: A
Molecule details ›
Chain: A
Length: 370 amino acids
Theoretical weight: 40.76 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
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

1 bound ligand:
Ligand MXT 2 x MXT
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: CONJOINED RIGID BODY/TORSION ANGLE SIMULATED ANNEALING DYNAMICS
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

41 review citations

The role of dynamic conformational ensembles in biomolecular recognition.
Boehr et al. (2009)
40 more

3 mentions without citation

Interplay between conformational selection and induced fit in multidomain protein-ligand binding probed by paramagnetic relaxation enhancement.
Clore GM. (2014)
2 more