Hong Zhang, Ph. D
 

 

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Associate Professor

Department of Biochemistry, L4.247B

University of Texas Southwestern Medical Center

5323 Harry Hines Blvd.

Dallas, Texas 75390-9038

Phone: 214-648-9299

Fax: 214-648-9099

Email: zhang@chop.swmed.edu


Education:

1986    B.S. in Biology, University of Science and Technology of China, Hefei, China.

1994    Ph.D. in Biophysics, University of Illinois at Urbana-Champaign, Urbana, IL.

 

Professional Experience:

9/86-5/89         Graduate research assistant, Institute of Biophysics, Chinese Academy of Sciences, Beijing, China. (Advisor: Prof. Dong-Cai Liang)

9/89-8/94         Graduate research assistant, Biophysics Division, University of Illinois at Urbana-Champaign, Urbana, IL. (Advisor: Prof. Andrew H.-J. Wang)

9/94-10/98       Howard Hughes Medical Institute postdoctoral research associate, University of Texas Southwestern Medical Center at Dallas. (Advisor: Prof. Johann Deisenhofer)

11/98-8/99       Research associate, Center for Advanced Research in Biotechnology, University of Maryland, Rockville, MD. (Advisor: Prof. Osnat Herzberg)

9/99-2/2005     Assistant Professor, Department of Biochemistry, UT Southwestern Medical Center at Dallas, TX.  

2/2005-present  Associate Professor, Department of Biochemistry, UT Southwestern Medical  Center at Dallas, TX.  

 

Publications:  

  31. Karthikeyan, S., Zhou, Q., Zhao, Z., Kao, C.-L., Tao, Z., Robinson, H., Liu H.-w. and Zhang, H.  (2004). Structural analysis of Pseudomonas 1-aminocyclopropane-1-carboxylate deaminase complexes: Insight into the mechanism of a unique pyridoxal-5’-phosphate dependent cyclopropane ring-opening reaction. Biochemistry, 43, 13328-13339.

  30. Ginalski, K, Zhang, H. and Grishin, N. V. (2004). Raptor protein contains a caspase-like domain. Trends in Biomed. Sci, 29, 522-524. 

  29. Karthikeyan, S., Zhao, Z., Kao, C., Zhou, Q., Tao, Z., Zhang, H. and Liu, H.-w. (2004).  Structural Analysis of 1-Aminocyclopropane-1-carboxylate Deaminase: Observation of an Aminyl Intermediate and Identification of Tyr294 as the Active-site Nucleophile.  Angew. Chem Int. Ed.. 43, 3425-3429.

  28. Zhang, H. (2004). Protein prenyltransferases. In Handbook of Metalloproteins, Volume 3. p37-48. A. Messerschmidt, W. Bode, and M.Cygler eds. (John Wiley & Sons). Invited book chapter.  

  27. Singh, S.K., Yang, K., Karthikeyan, S., Huynh, T., Zhang, X., Phillips, M. A., Zhang, H. (2004). The thrH gene product of Pseudomonas aeruginosa is a dual activity enzyme with a novel phosphoserine:homoserine phosphotransferase activity.  J. Biol. Chem. 279, 13166-13173. 

  26. Karthikeyan, S., Zhou, Q., Osterman, A. L. and Zhang, H. (2003) Ligand-binding induced conformational changes in riboflavin kinase: structural basis for the ordered mechanism.  Biochemistry, 42, 12532-12538.

  25. Zhang, H. (2003). Binding platforms for Rab prenylation and recycling: Rab escort protein, RabGGT and RabGDI.  Structure 11, 237-239.

  24. Zhang, X., Kurnasov, O. V., Karthikeyan, S., Grishin, N.V., Osterman, A. L. and Zhang, H. (2003). Structural characterization of a human cytosolic NMN/NaMN adenylyltransferase and implication in human NAD biosynthesis. J. Biol. Chem. 278, 13503-13511.

  23. Karthikeyan, S., Zhou, Q., Mseeh, F., Grishin, N. V., Osterman, A. L. and Zhang, H. (2003). Crystal structure of human riboflavin kinase reveals a b barrel fold and a novel active site arch. Structure 11, 265-273.

  22. Lim, K., Zhang, H., Toedt, J., Tempcyzk, A., Krajewski, W., Howard, A., Eisenstein, E., Herzberg, O. (2003). Structure of YibK methyltransferase from Haemophilus influenzae (HI0766): a cofactor bound at a site formed by a knot.  Proteins Struc. Func. and Genetics, 51, 56-67.

  21. Gilliland GL, Teplyakov A, Obmolova G, Tordova M, Thanki N, Ladner J, Herzberg O, Lim K, Zhang H, Huang K, Li Z, Tempczyk A, Krajewski W, Parsons L, Yeh DC, Orban J, Howard AJ, Eisenstein E, F Parsons J, Bonander N, Fisher KE, Toedt J, Reddy P, Rao CV, Melamud E, Moult J. (2002). Assisting functional assignment for hypothetical Heamophilus influenzae gene products through structural genomics. Curr Drug Targets Infect Disord. 2, 339-953.

  20. Chen, C. C., Zhang, H., Kim, A. D., Howard, A., Sheldrick, G. M., Mariano-Dunaway, D., Herzberg, O. (2002). Degradation Pathway of the Phosphonate Ciliatine: Crystal Structure of 2-Aminoethylphosphonate Transaminase. Biochemistry 41,13162-13169.

  19. Singh, S. K., Kurnasov, O. V., Chen, B., Robinson, H., Grishin, N. V., Osterman, A. L. and Zhang, H. (2002). Crystal structure of Haemophilus influenzae NadR protein: a bifunctional enzyme endowed with NMN adenylyltransferase and ribosylnicotinamide kinase activities. J. Biol. Chem., 277, 33291-33299.

  18. Cheek, S., Zhang, H. and Grishin, N. V. (2002). Sequence and Structure Classification of kinases. J. Mol. Biol. 320, 855-881.

  17. Zhou, T., Kurnasov, O. V., Tomchick, D., Binns, D., Grishin, N. V., Marquez, V. E., Osterman, A. L. and Zhang, H.. (2002). Structure of human nicotinamide/nicotinic acid mononucleotide adenylyltransferase: basis for the dual substrate specificity and activation of anticancer drug tiazofurin. J. Biol. Chem., 277, 13148-13154.

  16. Zhang, H., Zhou, T., Kurnasov, O. V., Cheek, S., Grishin, N. V. and Osterman, A. L. (2002). Crystal structure of E. coli nicotinate mononucleotide adenylyltransferase and its complex with deamido-NAD. Structure, 10, 69-79.

  15. Lim, K., Zhang, H., Tempczyk, A., Bonander, N., Toedt, J., Howard, A., Eisenstein, E. and Herzberg, O. (2001). Crystal Structure of YecO from Haemophilus influenzae (HI0319) reveals a methyltransferase fold and a bound S-adenosylhomocysteine. Proteins Struc. Func. and Genetics, 45, 397-407.

  14. Sri Krishna, S., Zhou, T., Daugherty, M., Osterman A. L. and Zhang, H. (2001). Structural basis for the catalysis and substrate specificity of homoserine kinase. Biochemistry, 40, 10810-10818.

  13. Zhou, T., Daugherty, M., Grishin, N. V., Osterman, A. L. and Zhang, H. (2000). Structure and Mechanism of Homoserine Kinase: prototype for GHMP kinase superfamily. Structure. 8, 1247-1257

(Works from graduate school and postdoc years)

  12. Zhang, H., Huang, K., Li, Zhong, Banerjee, L., Fisher, K., Eisenstein, E., Grishin, N. V. and Herzberg, O. (2000). Crystal structure of YbaK protein from Haemophilus influenzae at 1.8Å resolution: structure-functional implications. Proteins Struc. Func. and Genetics. 40, 86-97.

  11. Zhang, H., Seabra, M. and Deisenhofer, J. (2000). Crystal structure of Rab geranylgeranyl transferase at 2.0Å resolution. Structure. 8, 241-251.

  10. Zhang, H. and Grishin N. V. (1999). The a subunt of protein prenyltransferases is a member of the tetratricopeptide repeat family. Protein Science. 8, 1658-1667.

  9. Sevrioukova, I. F., Li, H., Zhang, H., Peterson, J. A. and Poulos, T. L. (1999). Structure of a cytochrome P450-redox partner electron-transfer complex. Proc. Natl. Acad. Sci. USA. 96, 1863-1868.

  8. Su, S., Gao, Y.G., Zhang, H., Terwilliger, T.C. and Wang, A.H.-J. (1997). Analysis of the stability and function of three surface mutants (R82C, K69H, and L32R) of the gene V protein from Ff phage by X-ray crystallography. Protein Science. 6:771-80

  7. Zhang, H., Skinner, M. M., Sandberg, W. S., Wang, A. H.-J. and Terwilliger, T. C. (1996). Context-dependence of mutational effects in a protein: the crystal structures of the V35I, I47V and V35I/I47V gene V protein core mutants. J. Mol. Biol. 259, 148-159.

  6. Guan, Y., Zhang, H. and Wang, A. H.-J. (1995). Electrostatic potential distribution of the gene V protein from Ff phage facilitates cooperative DNA binding: a model of the GVP-ssDNA complex. Protein Science. 4, 187-197.

  5. Guan, Y., Zhang, H., Konings, R. N. H., Hilbers, C. W., Terwilliger, T. C. & Wang, A. H.-J. (1994). Crystal structures of Y41H and Y41F mutants of gene V protein from Ff phage suggest possible protein-protein interactions in GVP-ssDNA complex. Biochemistry. 33, 7768-7778.

  4. Skinner, M. M., Zhang, H., Leschnitzer, D. H., Guan, Y., Bellamy, H., Sweet, R. M., Gray, C. W., Konings, R. N. H., Wang, A. H.-J. and Terwilliger, T. C. (1994). Structure of the gene V protein of bacteriophage f1 determined by multiwavelength X-ray diffraction on the selenomethionyl protein. Proc. Natl. Acad. Sci. USA. 91, 2071-2075.

  3. Zhang, H., Gao, Y.-G., van der Marel, G. A., van Boom, J. H. and Wang, A. H.-J. (1993). Simultaneous incorporation of two anticancer drugs into DNA: the structures of cross-linked adducts of Daunorubicin-d(CG(araC)GCG) and Doxrubicin-d(CA(araC)GTG) complexes at high resolution.  J. Biol. Chem. 268, 10095-10101.

  2. Wang, H.-J. A., Sriram, M., Gao, Y.- G., Robinson, H., Jean, Y.- C., Li, Y.- K. and Zhang, H. (1992). Anticancer drug daunorubicin and its derivatives can be crosslinked to DNA efficiently by formaldehyde: possible clues for drug design.  Structure & Function, Volume 1: Nucleic Acids. Eds. Sarma & Sarma, Adenine Press.

  1. Zhang, H., van der Marel, G. A., van Boom, J. H. and Wang, A. H.-J. (1992). Conformational perturbation of the anticancer nucleoside arabinosylcytosine on Z-DNA: molecular structure of (araC-dG)3 at 1.3 Å resolution.  Biopolymers. 32, 1559-1569.