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Education
Ph.D: Crystallography, University of Pittsburgh,
Pittsburgh, PA. U.S.A.
Current Research of Yuh-Ju Sun’s
Laboratory
Our laboratory uses X-ray crystallography method as a tool to
understand the structure and functions of various
biomacromolecules. The detail three-dimensional structure
information can be discovered and the structural biology studies
can be fully accomplished by computer modeling and simulation in
our laboratory. Meanwhile, the bioinformatics and the drug
design for clinical use, as novel therapeutics will also be
applied in our research. Our laboratory mainly focus in (1)
Structural genomic approach by X-ray crystallography; (2)
Structural and functional studies of Imidase by X-ray
crystallography.
I. Structural genomic study of
Helicobacter pylori by X-ray crystallography
Helicobacter pylori were identified as an etiologic agent in a
variety of gastroduodenal diseases and are the only
microorganism known to inhabit the human stomach. We will focus
on the hypothetical proteins of Helicobacter pylori, total about
three hundred proteins (208 hypothetical proteins with 50-200
amino acids and 99 hypothetical proteins with 200-500 amino
acids). We will clone and purify these target proteins and
determine its 3D structure by X-ray crystallography method. One
of the major goals of this structural functional genomics
project of Helicobacter pylori is to provide the significant
detail structure information in the drug design for the
application of Helicobacter pylori as a gastrointestinal
pathogen and to have a profound effect on current concepts of
gastric disease pathogenesis.
II. Structural and functional studies of Imidase by X-ray
crystallography
Imidase, an enzyme variously identified as
dihydropyrimidinase, hydantoinase, dihydropyrimidine hydrase,
and dihydropyrimidine amidohydrolase. Imidase is the second
enzyme involved in uracil and thymine catabolism. Imidase is
also involved in the degradation and biosynthesis of primidine.
The characteristic biological function of imidase is its broad
specificity for compounds in detoxication. Imidase is one family
of cyclic amidases produces the optically amino acids.
Therefore, the stereoselectivity or stereospecificity of imidase
to substract have the significance in industrial application.
Several investigations have found that a variety of proteins
have a significant sequence homology but lack a known functional
relationship with imidase. The studies suggest that some of
these proteins are important for neural growth and development.
We plan to do the structural basis study in Imidase and Imidase-substrate
complex from by X-ray Crystallography.
Teaching Activities
LS 452400/LS 452400-Biophysical Chemistry
LS 534800-Protein Structural and Functional Studies
LS 564700-Introduction of Structural Biology
LS 564600-X-ray Diffraction Analysis
LS 564300-Macromolecular Crystallography
LS 652100-Physical Biochemistry
LS 690102-Seminar
Papers Published within last 5 years
Chao,
T.-C., Huang, H., Tsai, J.-Y., Huang, C.-Y., and Sun, Y.-J..
Kinetic and structural properties of inorganic pyrophosphatase
from the pathogenic bacterium Helicobacter pylori. Proteins:
Structure, Function, and Bioinformatics (2006) 65, 670-80.
Lin,
Y.-F., Wu, M.-S., Chang, C.-C., Lin, S.-W., Lin, J.-T., Sun,
Y.-J., Chen, D.-S., and Chow, L.-P., Comparative
immunoproteomics of identification and characterization
virulence factors from Helicobacter pylori related to gastric
cancer. Mol Cell Proteomics. (2006) 8, p1484-96.
Huang,
C.-Y., Hsu, C.-H., Sun, Y.-J., Wu, H.-N., and Hsiao, C.-D.,
Complexed crystal structure of replication restart primosome
protein PriB reveals a novel single-stranded DNA-binding mode
Nucleic Acids Research, (2006), 34, 3878-86.
Tsai,
K. L., Huang, C.Y., Chang, C. H., Sun, Y.-J., Chuang, W. J.,
Hsiao, C.-D.. Crystal Structure of the Human FOXK1a-DNA
Complex and Its Implications on the Diverse Binding
Specificity of Winged Helix/Forkhead Proteins. J Biol Chem.
(2006) 281, 17400-9.
Tsai,
Y.-J., Chen, B.-T., Cheng, H.-C., Chen, H.-Y., Hsaio, N.-W.,
Lyu, P.-C. and Sun, Y.-J.. Crystal Structure of HP0242, a
Hypothetical Protein from Helicobacter pylori with a Novel
Fold. Proteins: Structure, Function, and Bioinformatics (2006)
62,1138-43.
Lee,
M. J., Huang, C. Y., Sun, Y.-J., and Huang, H. Cloning and
characterization of spermidine synthase and its implication in
polyamine biosynthesis in Helicobacter pylori strain 26695.
Protein Expr Purif. (2005) 43, 140-8.
Lu,
P.-K., Chien, S.-Y., Tsai, J.-Y., , Fong, C.-T., Lee, M.-J.,
Huang, H. and Sun, Y.-J.* Crystallization and Preliminary
X-ray Diffraction Analysis of Spermidine Synthase from
Helicobacter pylori Acta Cryst (2004) D60, 2067-2069.
Cheng,
H.-C., Cheng, P.-T., Peng, P., Lyu, P.-C. and Sun, Y.-J.,
Lipid Binding in Rice Nonspecific Lipid Transfer Protein-1
Complexes from Oryza sativa. Protein Sci. (2004) 13:
2304-2315.
Huang,
C.-Y., Huang, Chiang, S.-K., Chiang, Yang, Y.-S. and Sun,
Y.-J, Crystallization and Preliminary X-ray Diffraction
Analysis of Thermophilic Imidase from Pig Liver. Acta Cryst.
(2003) D59, 943-945.
Sun,Y.-J.,
Forouhar F, Li, H.-m., Tu, S.-L., Yeh, Y.-H., Kao, S, Shr,
H.-L., Chou, C.-C., Chen, Chinpan and Hsiao, C.-D. Crystal
structure of pea Toc34, a novel GTPase of the chloroplast
protein translocon. Nature Structure Biology (2002) 9:95-100.
Chou,C.-C.,
Wang C, Sun Y.-J., Shr, H.-L., Hsiao, C.-D., Crystallization
and preliminary X-ray diffraction analysis of the 10 kDa
C-terminal subdomain of 70 kDa heat-shock cognate protein.
Acta Cryst. (2001) D57,1928-30.
Hwang
S.-L., Cheng, T.-S., Chen, C.-H., Sun, Y.-J., Hsiao, C.-D.,
Hong, Y.-R. Boundary sequences of the NADPH oxidase p67(phox)
C-terminal SH3 domain play on its specificity. Biochem Biophys
Res Commun. (2001), 289(1):97-102
Sun,
Y.-J., Chang, N.-C. A., Hung, S.-I., Chien Chang, A., Chou,
C.-C. and Hsiao, C.-D. The crystal structure of a novel
mammalian lectin, Ym1, suggests a saccharide binding site. J.
Biol. Chem. (2001), 276, 17507-17514.
Liu,
J.-H. Liao, Y.-D. Sun, Y.-J., Crystallization and preliminary
X-ray diffraction analysis of cytotoxic ribonucleasesfrom
bullfrog Rana catesbeiana. Acta Cryst (2001) D57, 1697-1699.
Chou
C.-C., Sun Y.-J., Meng M.; Hsiao C.-D. The crystal structure
of phosphoglucose isomerase/autocrine motility factor/neuroleukin
complexed with its carbohydrate phosphate inhibitors suggests
its substrate/receptor recognition. J. Biol. Chem. (2000),
275:23154-60.
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