Ligand-induced conformational changes in a thermophilic ribose-binding protein (Q27652936)

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English	Ligand-induced conformational changes in a thermophilic ribose-binding protein	scientific article

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instance of

scholarly article

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title

Ligand-induced conformational changes in a thermophilic ribose-binding protein (English)

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main subject

structural biology

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author

Matthew J. Cuneo

series ordinal

1

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Lorena S. Beese

series ordinal

2

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Homme Hellinga

series ordinal

3

object named as

Homme W Hellinga

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publication date

19 November 2008

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published in

BMC Structural Biology

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volume

8

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issue

1

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page(s)

50

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cites work

The backbone structure of the thermophilic Thermoanaerobacter tengcongensis ribose binding protein is essentially identical to its mesophilic E. coli homolog

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Conformational changes of glucose/galactose-binding protein illuminated by open, unliganded, and ultra-high-resolution ligand-bound structures

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Specific recognition of saturated and 4,5-unsaturated hexuronate sugars by a periplasmic binding protein involved in pectin catabolism

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Crystal structures of an Extracytoplasmic Solute Receptor from a TRAP transporter in its open and closed forms reveal a helix-swapped dimer requiring a cation for alpha-keto acid binding

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X-ray structures of the leucine-binding protein illustrate conformational changes and the basis of ligand specificity

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Oxo-iron clusters in a bacterial iron-trafficking protein: new roles for a conserved motif

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Crystal structures of the liganded and unliganded nickel-binding protein NikA from Escherichia coli

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Competitive antagonism of AMPA receptors by ligands of different classes: crystal structure of ATPO bound to the GluR2 ligand-binding core, in comparison with DNQX

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Structural identification of a bacterial quorum-sensing signal containing boron

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Evidence for lateral gene transfer between Archaea and Bacteria from genome sequence of Thermotoga maritima

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Structure of D-allose binding protein from Escherichia coli bound to D-allose at 1.8 A resolution

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Multiple open forms of ribose-binding protein trace the path of its conformational change

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The structure of glutamine-binding protein complexed with glutamine at 1.94 A resolution: comparisons with other amino acid binding proteins

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Structure of Haemophilus influenzae Fe(+3)-binding protein reveals convergent evolution within a superfamily

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Extensive features of tight oligosaccharide binding revealed in high-resolution structures of the maltodextrin transport/chemosensory receptor

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Peptide Binding in OppA, the Crystal Structures of the Periplasmic Oligopeptide Binding Protein in the Unliganded Form and in Complex with Lysyllysine,

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The crystal structure of glutamine-binding protein from Escherichia coli

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Modulation of a salt link does not affect binding of phosphate to its specific active transport receptor

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2 A resolution structure of DppA, a periplasmic dipeptide transport/chemosensory receptor

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Three-dimensional structures of the periplasmic lysine/arginine/ornithine-binding protein with and without a ligand

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Probing protein-protein interactions. The ribose-binding protein in bacterial transport and chemotaxis

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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

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Identifiers

DOI

10.1186/1472-6807-8-50

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Dimensions Publication ID

1029146385

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Fatcat ID

release_m7fxormtuve6blkdp5npvdbsd4

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PMC publication ID

2630998

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PubMed publication ID

19019243

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ResearchGate publication ID

23483323

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