Abstract

Receptors are key molecules that recognize the target molecule on the extracellular side of the cell and initiate a series of downstream intracellular processes. Bacterial receptors have similar domain structures as many mammalian hormone receptors in that they have ligand binding components on the extracellular side, transmembrane components which span the membrane, and cytoplasmic components for effector binding inside the cell. Two receptor systems will be studied using X-ray crystallographic methods: (1) Bacterial aspartate receptor for chemotaxis in Salmonella and E.coli. (2) Two transport receptors from Salmonella, one for transport of the amino acid histidine and the other for transport of lysine/arginine/ornithine. Our overall objective is to determine the three-dimensional structure of the components and domains of these bacterial receptors. This would enable us to understand the signal transduction mechanism of chemotaxis and amino acid transport including the ligand recognition, signal transduction through the transmembrane and adaptation at the cytoplasmic domain. We have so far crystallized three proteins: the ligand binding domain of aspartate receptor and two amino acid receptors: one for histidine transport and the other for lysine/arginine/ ornithine transport.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of Allergy and Infectious Diseases (NIAID)
Type
Research Project (R01)
Project #
1R01AI030725-01
Application #
3145765
Study Section
Biophysical Chemistry Study Section (BBCB)
Project Start
1991-02-01
Project End
1996-01-31
Budget Start
1991-02-01
Budget End
1992-01-31
Support Year
1
Fiscal Year
1991
Total Cost
Indirect Cost

  Institution

Name
University of California Berkeley
Department
Type
Schools of Arts and Sciences
DUNS #
094878337
City
Berkeley
State
CA
Country
United States
Zip Code
94704

  Publications

Yeh, J I; Biemann, H P; Prive, G G et al. (1996) High-resolution structures of the ligand binding domain of the wild-type bacterial aspartate receptor. J Mol Biol 262:186-201
Wolf, A; Shaw, E W; Oh, B H et al. (1995) Structure/function analysis of the periplasmic histidine-binding protein. Mutations decreasing ligand binding alter the properties of the conformational change and of the closed form. J Biol Chem 270:16097-106
Oh, B H; Ames, G F; Kim, S H (1994) Structural basis for multiple ligand specificity of the periplasmic lysine-, arginine-, ornithine-binding protein. J Biol Chem 269:26323-30
Jamieson, A C; Kim, S H; Wells, J A (1994) In vitro selection of zinc fingers with altered DNA-binding specificity. Biochemistry 33:5689-95
Kim, S H (1994) ""Frozen"" dynamic dimer model for transmembrane signaling in bacterial chemotaxis receptors. Protein Sci 3:159-65
Oh, B H; Kang, C H; De Bondt, H et al. (1994) The bacterial periplasmic histidine-binding protein. structure/function analysis of the ligand-binding site and comparison with related proteins. J Biol Chem 269:4135-43
Oh, B H; Pandit, J; Kang, C H et al. (1993) Three-dimensional structures of the periplasmic lysine/arginine/ornithine-binding protein with and without a ligand. J Biol Chem 268:11348-55
Yeh, J I; Biemann, H P; Pandit, J et al. (1993) The three-dimensional structure of the ligand-binding domain of a wild-type bacterial chemotaxis receptor. Structural comparison to the cross-linked mutant forms and conformational changes upon ligand binding. J Biol Chem 268:9787-92
Scott, W G; Milligan, D L; Milburn, M V et al. (1993) Refined structures of the ligand-binding domain of the aspartate receptor from Salmonella typhimurium. J Mol Biol 232:555-73
Kim, S H; Prive, G G; Yeh, J et al. (1992) A model for transmembrane signaling in a bacterial chemotaxis receptor. Cold Spring Harb Symp Quant Biol 57:17-24

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