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Structural
biology, structural genomics, DNA repair, NMR-based metabonomics, NMR
spectroscopy, x-ray crystallography
My research involves the use of nuclear magnetic
resonance spectroscopy (NMR) and x-ray crystallography to study the
structure and function of proteins important to human health, host
pathogen interactions, and novel metabolic pathways in exotic bacteria.
We have particular interest in molecular mechanisms of human DNA repair,
gene regulation in human adaptive immune responses, and NMR-based
metabonomics to study several human diseases, including ovarian cancer
and biliary atresia. My group is also part of a Large Scale Production
Center for Structural Genomics funded by the National Institutes of
Health’s Protein Structure Initiative whose goal is to make the
three-dimensional structure of all proteins easily available from
knowledge their amino acid sequences. Structural genomics requires
high throughput protein structure determination using NMR and x-ray
crystallography.
Recent Publications
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T.A. Ramelot, J.
R. Cort, S. Goldsmith-Fischman, G.J. Kornhaber, R. Xiao, R. Shastry,
T. B. Acton, B. Honig, G.T. Montelione, and M.A. Kennedy “Solution
NMR Structure of the Iron-Sulfur Cluster Assembly Protein U (IscU)
with Zinc Bound at the Active Site” Journal of Molecular
Bioliology, 344, 567-83, 2004.
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S. Ni, H.
Robinson, C.G. Marsing, D.E. Bussiere, and M.A. Kennedy “Structure
of 2C-Methyl-D-erythritol-2,4-cyclodiphosphate Synthase from
Shewanella oneidensis at 1.6Å: Identification of Farnesyl
Diphosphate Trapped in a Hydrophobic Cavity” Acta
Crystallographica Section D, 60,1949-57, 2004.
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G.W. Buchko, K.
McAteer, S.S. Wallace, and M.A. Kennedy “Solution-State NMR
Investigation of DNA Binding Interactions in Escherichia coli
formamidopyrimidine-DNA glycosylase (Fpg): A Dynamic Description of
the DNA /Protein Interface” DNA Repair, 4, 327-339, 2005.
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S.
Ni, F. Farouhar, H. Robinson, D. E. Bussiere, and M.A. Kennedy
(2005) "Structure Determination of VC0702 at 2.0Å, a Conserved
Hypothetical Protein from Vibrio Cholerae” Proteins:
Structure, Function, Bioinformatics, 63, 733-741, 2006.
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G.W. Buchko, S.
Ni, H. Robinson, E. Welsh, H.Pakrasi, and M.A. Kennedy
“Characterization of two potentially universal turn motifs that
shape the repeated five residues fold- Crystal structure
of a lumenal pentapeptide repeat protein from Cyanothece
51142” Protein Science, 2006.
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T.A. Ramelot, A.
Yee, J.R. Cort, A. Semesi, C.A. Arrowsmith, and M.A. Kennedy “NMR
Structure and Binding Studies Confirm that PA4608 from
Pseudomonas aeruginosa is a PilZ Domain and a c-di-GMP Binding
Protein” Proteins: Structure, Function, and Bioinformatics,
2006.
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G.W. Buchko,
Chang Y. Kim, Thomas C. Terwilliger, and Michael A. Kennedy
“Solution Structure of the Conserved Hypothetical Protein Rv2302
from Mycobacterium tuberculosis” J. Bacteriology, 188,
5993-6001 (2006).
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