The goal of this Program Project application is to assign structure and function to the protein products of genomic open reading frames for which there are no homologues with known three dimensional structure and function. In a departure from current practice, the applicant and his project leaders are proposing to mount a comprehensive, concerted effort, using high throughput crystallographic approaches, to determine protein function from atomic level structure. Complementary DNA from selected Hemophilus influenzae genes, and other microorganisms as indicated, will be cloned for expression in Escherichia coli and purification of the protein products in order to obtain sufficient quantities of protein for crystallization and X-ray crystallographic and NMR 3D structure determinations.

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Program Projects (P01)
Project #
5P01GM057890-04
Application #
6386944
Study Section
Special Emphasis Panel (ZRG3-SSS-2 (05))
Program Officer
Norvell, John C
Project Start
1998-08-01
Project End
2003-07-31
Budget Start
2001-08-01
Budget End
2002-07-31
Support Year
4
Fiscal Year
2001
Total Cost
$952,507
Indirect Cost
Name
University of MD Biotechnology Institute
Department
Type
Organized Research Units
DUNS #
City
Baltimore
State
MD
Country
United States
Zip Code
21202
Zhao, Hong; Lim, Kap; Choudry, Anthony et al. (2012) Correlation of structure and function in the human hotdog-fold enzyme hTHEM4. Biochemistry 51:6490-2
Chen, Chen; Gorlatova, Natalia; Kelman, Zvi et al. (2011) Structures of p63 DNA binding domain in complexes with half-site and with spacer-containing full response elements. Proc Natl Acad Sci U S A 108:6456-61
Lim, Kap; Pullalarevu, Sadhana; Surabian, Karen Talin et al. (2010) Structural basis for the mechanism and substrate specificity of glycocyamine kinase, a phosphagen kinase family member. Biochemistry 49:2031-41
Chen, Chen; Sun, Qihong; Narayanan, Buvaneswari et al. (2010) Structure of oxalacetate acetylhydrolase, a virulence factor of the chestnut blight fungus. J Biol Chem 285:26685-96
Melamud, Eugene; Moult, John (2009) Stochastic noise in splicing machinery. Nucleic Acids Res 37:4873-86
Melamud, Eugene; Moult, John (2009) Structural implication of splicing stochastics. Nucleic Acids Res 37:4862-72
Chao, Kinlin L; Lim, Kap; Lehmann, Christopher et al. (2008) The Escherichia coli YdcF binds S-adenosyl-L-methionine and adopts an alpha/beta-fold characteristic of nucleotide-utilizing enzymes. Proteins 72:506-9
Zhuang, Zhihao; Song, Feng; Zhao, Hong et al. (2008) Divergence of function in the hot dog fold enzyme superfamily: the bacterial thioesterase YciA. Biochemistry 47:2789-96
Willis, Mark A; Zhuang, Zhihao; Song, Feng et al. (2008) Structure of YciA from Haemophilus influenzae (HI0827), a hexameric broad specificity acyl-coenzyme A thioesterase. Biochemistry 47:2797-805
Sari, Nese; He, Yanan; Doseeva, Victoria et al. (2007) Solution structure of HI1506, a novel two-domain protein from Haemophilus influenzae. Protein Sci 16:977-82

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