1OMP

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

Summary for 1OMP

• Entry DOI: 10.2210/pdb1omp/pdb
• Descriptor: D-MALTODEXTRIN BINDING PROTEIN (2 entities in total)
• Functional Keywords: periplasmic binding protein
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 40753.15

Authors

Sharff, A.J.,Quiocho, F.A. (deposition date: 1992-09-14, release date: 1994-01-31, Last modification date: 2024-02-14)

Primary citation

Sharff, A.J.,Rodseth, L.E.,Spurlino, J.C.,Quiocho, F.A.
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.
Biochemistry, 31:10657-10663, 1992

PubMed Abstract: 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.

PubMed: 1420181
DOI: 10.1021/bi00159a003

Experimental method

X-RAY DIFFRACTION (1.8 Å)