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PDBsum entry 1omp
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Periplasmic binding protein
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PDB id
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1omp
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References listed in PDB file
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Key reference
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Title
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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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Authors
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A.J.Sharff,
L.E.Rodseth,
J.C.Spurlino,
F.A.Quiocho.
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Ref.
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Biochemistry, 1992,
31,
10657-10663.
[DOI no: ]
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PubMed id
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Abstract
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The periplasmic maltodextrin binding protein of Escherichia coli serves as an
initial receptor for the active transport of and chemotaxis toward
maltooligosaccharides. The three-dimensional structure of the binding protein
complexed with maltose has been previously reported [Spurlino, J. C., Lu, G.-Y.,
& Quiocho, F. A. (1991) J. Biol. Chem. 266, 5202-5219]. Here we report the
structure of the unliganded form of the binding protein refined to 1.8-A
resolution. This structure, 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. The unliganded structure shows a
rigid-body "hinge-bending" between the two globular domains by approximately 35
degrees, relative to the maltose-bound structure, opening the sugar binding site
groove located between the two domains. In addition, there is an 8 degrees twist
of one domain relative to the other domain. The conformational changes observed
between this structure and the maltose-bound structure are consistent with
current models of maltose/maltodextrin transport and maltose chemotaxis and
solidify a mechanism for receptor differentiation between the ligand-free and
ligand-bound forms in signal transduction.
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Secondary reference #1
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Title
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Three-Dimensional structure of recombinant human muscle fatty acid-Binding protein.
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Authors
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G.Zanotti,
G.Scapin,
P.Spadon,
J.H.Veerkamp,
J.C.Sacchettini.
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Ref.
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J Biol Chem, 1992,
267,
18541-18550.
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PubMed id
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Secondary reference #2
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Title
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The 2.3-A resolution structure of the maltose- Or maltodextrin-Binding protein, A primary receptor of bacterial active transport and chemotaxis.
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Authors
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J.C.Spurlino,
G.Y.Lu,
F.A.Quiocho.
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Ref.
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J Biol Chem, 1991,
266,
5202-5219.
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PubMed id
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