Effects of ligand binding on the internal dynamics of maltose-binding protein.

@article{Dring1999EffectsOL,
  title={Effects of ligand binding on the internal dynamics of maltose-binding protein.},
  author={Klaus D{\"o}ring and Thomas Surrey and Peter San Francisco Nollert and Fritz J{\"a}hnig},
  journal={European journal of biochemistry},
  year={1999},
  volume={266 2},
  pages={
          477-83
        }
}
Ligand binding to proteins often causes large conformational changes. A typical example is maltose-binding protein (MBP), a member of the family of periplasmic binding proteins of Gram-negative bacteria. Upon binding of maltose, MBP undergoes a large structural change that closes the binding cleft, i.e. the distance between its two domains decreases. In contrast, binding of the larger, nonphysiological ligand beta-cyclodextrin does not result in closure of the binding cleft. We have… 
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References

SHOWING 1-10 OF 27 REFERENCES
Two modes of ligand binding in maltose-binding protein of Escherichia coli. Electron paramagnetic resonance study of ligand-induced global conformational changes by site-directed spin labeling.
TLDR
The present work suggests that the B mode is nonproductive because ligands binding in this manner prevent the closure of the two domains of MBP, and, as a result, the resulting ligand-MBP complex is incapable of interacting properly with the inner membrane-associated transporter complex.
Two modes of ligand binding in maltose-binding protein of Escherichia coli. Correlation with the structure of ligands and the structure of binding protein.
TLDR
UV differentialSpectroscopy and fluorescence emission spectroscopy were used to study the modes by which various ligands bind to MBP and found that ligands that are bound exclusively via the B mode to either the wild type or MalE254 MBP are not transported.
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.
TLDR
The structure of the unliganded form of the binding protein refined to 1.8-A resolution, combined with that for the liganded form, provides the first crystallographic evidence that a major ligand-induced conformational change occurs in a periplasmic binding protein.
Conformational changes of three periplasmic receptors for bacterial chemotaxis and transport: the maltose-, glucose/galactose- and ribose-binding proteins.
TLDR
Small-angle X-ray scattering experiments were carried out for the maltose-binding protein, providing evidence that a large conformational change takes place in association with ligand binding to the glucose/galactose- and ribose- binding proteins, and that the two changes are similar.
Multiple open forms of ribose-binding protein trace the path of its conformational change.
TLDR
Three open, ligand-free forms of the Escherichia coli ribose-binding protein were observed here by X-ray crystallographic studies, and it seems certain that the conformational path that links the forms described here is that followed during ligand retrieval, and in ligand release into the membrane-bound permease system.
Rates of ligand binding to periplasmic proteins involved in bacterial transport and chemotaxis.
The structural basis of sequence-independent peptide binding by OppA protein.
TLDR
The oligopeptide-binding protein of Salmonella typhimurium (OppA) binds peptides of two to five amino acid residues without regard to sequence, unlike other periplasmic binding proteins.
The 2.3-A resolution structure of the maltose- or maltodextrin-binding protein, a primary receptor of bacterial active transport and chemotaxis.
The three-dimensional structure of the maltose- or maltodextrin-binding protein (Mr = 40,622) with bound maltose has been obtained by crystallographic analysis at 2.8-A resolution. The structure,
Refined 1.8-A structure reveals the mode of binding of beta-cyclodextrin to the maltodextrin binding protein.
TLDR
The observed structure shows that the complexed protein remains in the fully open conformation and is almost identical to the structure of the unliganded protein, which is not a physiological ligand for the maltodextrin binding protein.
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