Crystallography is the predominant method by which structural information at atomic resolution on large (> 40 kD) protein molecules can be obtained. Such information is key to understanding the function of proteins, and a basis for the design of mutants and drugs.
We have crystallized and determined the 3-D structures of water-soluble proteins and integral membrane proteins. Main criteria for selection of proteins are their biological significance, unusual amino acid sequences, and involvement in electron transfer or energy transfer processes. Current projects include: iron transporters from the outer membrane of gram-negative bacteria, HMG-CoA reductase, the extracellular portion of the LDL receptor, proteins related to the control of gene expression in response to intracellular cholesterol levels, the light activated DNA repair enzyme photolyase in a complex with a substrate, photolyase-related blue light photorecptors, the neural proteins synapsin and neurexin 1, the mitochondrial processing peptidase from yeast.
RECENT PUBLICATIONS
A.D. Ferguson, C.A. Amezcua, N.M. Halabi, Y. Chelliah, M.K. Rosen, R. Ranganathan, J. Deisenhofer, "Signal transduction pathway of TonB-dependent transporters." Proc. Natl. Acad. Sci. USA, 104 (2):513-518, January 2007
Y. Huang, R. Baxter, B. Smith, C. Partch, C. Colbert, J. Deisenhofer, "Crystal structure of cryptochrome 3 from Arabidopsis thaliana and its implications for photolyase activity." Proc. Natl. Acad. Sci. USA, 103 (47):17701-17706, November 2006
C.-I. Chang, Y. Chelliah, D. Borek, D. Mengin-Lecreulx & J. Deisenhofer, "Structure of tracheal cytotoxin in complex with a heterodimeric pattern-recognition receptor." Science, 311 (5768):1761-1764, March 2006
A.D. Ferguson, V.M. Labunskyy, D.E. Fomenko, Y. Chelliah, D. Arac, C.A. Amezcua, J. Rizo, V.N. Gladyshev & J. Deisenhofer, "NMR structures of the selenoproteins Sep15 and SelM reveal redox activity of a new thioredoxin-like family." J. Biol. Chem, 281 (6):3536-3543, February 2006
R. H. G. Baxter, C.-I. Chang, Y. Chelliah, S. Blandin, E. A. Levashina, J. Deisenhofer, "Structural basis for conserved complement factor-like function in the antimalarial protein TEP1." Proc. Natl. Acad. Sci. USA, 104 (28):11615-11620, July 2007
SIGNIFICANT PUBLICATIONS
Rudenko, G., Henry, L., Henderson, K., Ichtchenko, K., Brown, M.S., Goldstein, J.L., and Deisenhofer, J., "Structure of the LDL receptor extracellular domain at endosomal pH." Science, 298:2353-2358, 2002
D. Xia, C.-A. Yu, H. Kim, J.-Z. Xia, A.M. Kachurin, L. Zhang, L. Yu & J. Deisenhofer, "The crystal structure of the cytochrome bc1 complex from bovine heart mitochondria." Science, 277:60-66, 1997
B. Kobe & J. Deisenhofer, "Crystal structure of porcine ribonuclease inhibitor, a protein with leucine-rich repeats." Nature, 366:751-756, 1993
J. Deisenhofer & H. Michel, "The photosynthetic reaction centre from the purple bacterium Rhodopseudomonas viridis." EMBO J, 8 (8):2149-2170, 1989
Deisenhofer, J., and Steigemann, W., "Crystallographic refinement of the structure of bovine pancreatic trypsin inhibitor at 1.5 A-prime resolution." Acta Crystallographica, B31:238-250, 1975
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