Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
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Journal
IF	>30 >20 >10 >5 all

Title	Crystal structures of the maltodextrin/maltose-binding protein complexed with reduced oligosaccharides: flexibility of tertiary structure and ligand binding.
Journal, issue, pages	J. Mol. Biol., Vol. 306, Page 1115-1126, Year 2001
Publish date	Sep 4, 2000 (structure data deposition date)
Authors	X Duan / J A Hall / H Nikaido / F A Quiocho /
PubMed Abstract	The structure of the maltodextrin or maltose-binding protein, an initial receptor for bacterial ABC-type active transport and chemotaxis, consists of two globular domains that are separated by a ...The structure of the maltodextrin or maltose-binding protein, an initial receptor for bacterial ABC-type active transport and chemotaxis, consists of two globular domains that are separated by a groove wherein the ligand is bound and enclosed by an inter-domain rotation. Here, we report the determination of the crystal structures of the protein complexed with reduced maltooligosaccharides (maltotriitol and maltotetraitol) in both the "closed" and "open" forms. Although these modified sugars bind to the receptor, they are not transported by the wild-type transporter. In the closed structures, the reduced sugars are buried in the groove and bound by both domains, one domain mainly by hydrogen-bonding interactions and the other domain primarily by non-polar interactions with aromatic side-chains. In the open structures, which abrogate both cellular activities of active transport and chemotaxis because of the large separation between the two domains, the sugars are bound almost exclusively to the domain rich in aromatic residues. The binding site for the open chain glucitol residue extends to a subsite that is distinct from those for the glucose residues that were uncovered in prior structural studies of the binding of active linear maltooligosaccharides. Occupation of this subsite may also account for the inability of the reduced oligosaccharides to be transported. The structures reported here, combined with those previously determined for several other complexes with active oligosaccharides in the closed form and with cyclodextrin in the open form, revealed at least four distinct modes of ligand binding but with only one being functionally active. This versatility reflects the flexibility of the protein, from very large motions of interdomain rotation to more localized side-chain conformational changes, and adaptation by the oligosaccharides as well.
External links	J. Mol. Biol. / PubMed:11237621
Methods	X-ray diffraction
Resolution	1.9 - 2.3 Å
Structure data	PDB-1fqa: STRUCTURE OF MALTOTETRAITOL BOUND TO OPEN-FORM MALTODEXTRIN BINDING PROTEIN IN P2(1)CRYSTAL FORM Method: X-RAY DIFFRACTION / Resolution: 1.9 Å PDB-1fqb: STRUCTURE OF MALTOTRIOTOL BOUND TO OPEN-FORM MALTODEXTRIN BINDING PROTEIN IN P2(1)CRYSTAL FORM Method: X-RAY DIFFRACTION / Resolution: 1.9 Å PDB-1fqc: CRYSTAL STRUCTURE OF MALTOTRIOTOL BOUND TO CLOSED-FORM MALTODEXTRIN BINDING PROTEIN Method: X-RAY DIFFRACTION / Resolution: 2.3 Å PDB-1fqd: CRYSTAL STRUCTURE OF MALTOTETRAITOL BOUND TO CLOSED-FORM MALTODEXTRIN BINDING PROTEIN Method: X-RAY DIFFRACTION / Resolution: 2.3 Å
Chemicals	ChemComp-HOH: WATER
Source	escherichia coli (E. coli)
Keywords	SUGAR BINDING PROTEIN / sugar-binding protein / maltotetraitol / maltotriotal / maltotriotol