Crystal stuctures of MglB-2 (TP0684), a topologically variant d -glucose-binding protein from Treponema pallidum, reveal a ligand-induced conformational change

Author:

Brautigam Chad A.12,Deka Ranjit K.2,Liu Wei Z.2,Norgard Michael V.2

Affiliation:

1. Department of Biophysics; The University of Texas Southwestern Medical Center; Dallas Texas 75390

2. Department of Microbiology; The University of Texas Southwestern Medical Center; Dallas Texas 75390

Funder

National Institutes of Health

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Reference20 articles.

1. ABC transporters: how small machines do a big job;Davidson;Trends Microbiol,2007

2. Atomic structure and specificity of bacterial periplasmic receptors for active transport and chemotaxis: variation of common themes;Quiocho;Mol Microbiol,1996

3. Hinge-bending in L-Arabinose- binding protein: the “Venus-flytrap” model;Mao;J Biol Chem,1982

4. The calcium-binding site in the galactose chemoreceptor protein. Crystallographic and metal-binding studies;Vyas;J Biol Chem,1989

5. Sugar and signal-transducer binding sites of the Escherichia coli galactose chemoreceptor protein;Vyas;Science,1988

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