Abstract

This core project will provide NMR data on some members of the set of expressed H. influenzae proteins that will be provided by other components of the project. NMR will be used in early stages to screen conditions for solubility (in states of low aggregation), and the degree of folding of the protein. When suitable conditions are found, labeled protein will be generated and resonance assignments will be determined using multi-nuclear multi-dimensional methods. With backbone assignments, a quick assessment of secondary structure can be made, which will feed into the structure prediction effort. Further analysis of NMR data will then lead to identification of the fold (a low resolution structure), and can be pushed on to give high resolution structure when desired. The effort will be guided by Dr. Organ, and largely executed by one Research Associate (Dr. Sari), with about 1/2 of a 600 MHz spectrometer dedicated to the work. The expected culprit will be the order of 2 low resolution and 1 high-resolution structure per year.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Program Projects (P01)
Project #
5P01GM057890-02
Application #
6204324
Study Section
Project Start
1999-08-01
Project End
2000-07-31
Budget Start
1997-10-01
Budget End
1998-09-30
Support Year
2
Fiscal Year
1999
Total Cost
Indirect Cost

  Institution

Name
University of MD Biotechnology Institute
Department
Type
DUNS #
City
Baltimore
State
MD
Country
United States
Zip Code
21202

  Publications

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

Showing the most recent 10 out of 52 publications