Gregory A. Grant, Ph.D.

Professor
Internal Medicine
Dermatology
Developmental Biology

Biochemistry, Biophysics, and Structural Biology Program
Molecular Cell Biology Program

  • 314-362-3367

  • 314-362-3352

  • 314-362-4698

  • 8103

  • 3830 North Building

  • ggrant@wustl.edu

  • http://devbio.wustl.edu/faculty/faculty-members/gregory-a.-grant

  • protein structure, protein function, allosteric regulation, enzymology, biochemistry

  • Relationship of structure to function in allosteric control mechanisms

Research Abstract:

The main focus of the laboratory is the structural basis of allosteric control and its long-term application to understanding control processes resulting from protein-ligand and protein-protein interactions. This research focuses on enzymatic regulatory mechanisms that involve the ACT domain and ASB domains. The ACT domain is a structural motif widely employed in the regulation of protein activity by small molecules. The ASB domain is often found in tandem with an ACT domain. Major techniques utilized will be site-directed mutagenesis, steady-state and transient kinetic analysis, and fluorescent techniques. X-ray crystallography is also employed on a collaborative basis. These studies are an integral step in the long term goals of this laboratory: to determine the relationship between structure and function in conformationally regulated control mechanisms; to eventually relate that to the physiology and pathophysiology mediated by these enzymes and by analogous systems; and to eventually understand allosteric proteins well enough to be able to apply basic principles to more complex systems.

Selected Publications:

Grant GA. Contrasting Catalytic and Allosteric Mechanisms for Phosphoglycerate Dehydrogenases. Arch. Biochem. Biophys. (2012) 519, 175-185.

Chen,S., Xu, X. L., and Grant, G.A. (2012) Allosteric Activation and Contrasting Properties of Types 1 and 2 L-Serine Dehydratases, Biochemistry, 51, 5320-5328.PMID:22686449

Xu XL, Chen S and Grant GA. Kinetic, Mutagenesis, and Structural Homology Analysis of L-Serine Dehydratase from Legionella pneumophila. Archives of Biochemistry and Biophysics 2011 515(1-2): 28-36. PMID:21878319

Grant GA. Transient Kinetic Analysis of L-Serine Interaction with E. coli D-3-Phosphoglycerate Dehydrogenase Containing Amino Acid Mutations in the Hinge Region. Biochemistry 2011 50:2900-2906. PMCID: PMC3071459

Burton RL, Chen S, Xu XL and Grant GA. Transient kinetic analysis of L-serine interaction with E. coli D-3-phosphoglycerate dehydrogenase reveals the mechanism of V-type regulation and the order of effector binding. 2009 48: 12242-12251. PMCID: PMC2797576

Burton RL, Chen S, Xu XL and Grant GA. Role of the anion binding site in catalysis and regulation of Mycobacterium tuberculosis D-3-phosphoglycerate dehydrogenase. Biochemistry 2009 48: 4808-4815.PMCID: PMC2692652

Burton RL, Hanes JW and Grant GA. A stopped-flow kinetic analysis of substrate binding and catalysis in E. coli D-3-Phoshphoglycerate Dehydrogense. J. Biol. Chem. 2008 283: 29706-29714.PMCID: PMC2573093

Dey S, Burton RL, Grant GA and Sacchettini JC. Structural analysis of substrate and effector binding in Mycobacterium tuberculosis D-3-phosphoglycerate dehydrogenase. Biochemistry 2008 47: 8721-8282.PMCID: PMC2551328

Burton RL, Chen S, Xu XL and Grant GA. A Novel Mechanism for Substrate Inhibition in Mycobacterium tuberculosis D-3-Phosphoglycerate Dehydrogenase. J Biol Chem 2007 282: 31493-31503.PMID:17761677

Last Updated: 7/11/2016 2:45:44 PM

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