Watching a protein as it functions with 150-ps time-resolved x-ray crystallography

Science

Volumn 300, Issue 5627, 2003, Pages 1944-1947

  Schotte, Friedrich ^a   Lim, Manho ^b   Jackson, Timothy A ^c   Smirnov, Aleksandr V ^a   Soman, Jayashree ^d   Olson, John S ^d   Phillips Jr , George N ^e   Wulff, Michael ^f   Anfinrud, Philip A ^a  

^a NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES   (United States)

^b Pusan National University   (South Korea)

^c HARVARD MEDICAL SCHOOL   (United States)

^d RICE UNIVERSITY   (United States)

^e UNIVERSITY OF WISCONSIN MADISON   (United States)

^f EUROPEAN SYNCHROTRON RADIATION FACILITY   (France)

Author keywords

[No Author keywords available]

Indexed keywords

CARBON MONOXIDE; CARRIER CONCENTRATION; CONFORMATIONS; INFRARED SPECTROSCOPY; MOLECULAR STRUCTURE; PHOTOLYSIS; X RAY DIFFRACTION ANALYSIS;

MYOGLOBIN;

PROTEINS;

CARBOXYMYOGLOBIN; HEME; HISTIDINE; ISOLEUCINE; LEUCINE; MUTANT PROTEIN; MYOGLOBIN; PHENYLALANINE; VALINE;

BIOCHEMISTRY; PROTEIN;

ARTICLE; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; ELECTRON; ENERGY; INFRARED SPECTROSCOPY; MOLECULAR DYNAMICS; PHOTOLYSIS; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN STRUCTURE; TIME; X RAY CRYSTALLOGRAPHY; X RAY DIFFRACTION;

AMINO ACID SUBSTITUTION; ANIMALS; BINDING SITES; CARBON MONOXIDE; CRYSTALLOGRAPHY, X-RAY; FOURIER ANALYSIS; HEME; LIGANDS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; MYOGLOBIN; PHOTOLYSIS; PROTEIN CONFORMATION; SPECTROPHOTOMETRY, INFRARED; TIME FACTORS; WHALES;

EID: 0038047431     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.1078797     Document Type: Article

References (25)

1. As of July 2002, more than 12,000 protein structures have been deposited into the Protein Data Bank, of which nearly 3300 are characterized as enzymes [H. M. Berman et al., Nucleic Acids Res. 28, 235 (2000)].
2. R. H. Austin, K. W. Beeson, L. Eisenstein, H. Frauenfelder, I. C. Gunsalus, Biochemistry 14, 5355 (1975).
3. A. Ansari, C. M. Jones, E. R. Henry, J. Hofrichter, W. A. Eaton, Biochemistry 33, 5128 (1994).
4. T. A. Jackson, M. Lim, P. A. Anfinrud, Chem. Phys. 180, 131 (1994).
5. X. Ye, A. Demidov, P. M. Champion, J. Am. Chem. Soc. 124, 5914 (2002).
6. M. H. Lim, T. A. Jackson, P. A. Anfinrud, J. Chem. Phys. 102, 4355 (1995).
7. D. Vitkup, G. A. Petsko, M. Karplus, Nature Struct. Biol. 4, 202 (1997).
8. I. Schlichting, J. Berendzen, G. N. Phillips Jr., R. M. Sweet, Nature 371, 808 (1994).
9. T. Y. Teng, V. Srajer, K. Moffat, Nature Struct. Biol. 1, 701 (1994).
10. T. E. Carver et al., J. Biol. Chem. 1992, 14443 (1992).
11. Materials and methods are available as supporting material on Science Online.
12. We believe that the extrapolated electron density maps presented here are more informative than difference electron density maps. With difference maps, only those structural changes whose difference density rises above a specified threshold (contour level) are observable. Moreover, those features are only rarely centered on the atoms that move, which makes it more difficult to visualize the atomic motion.
13. M. Lim, T. A. Jackson, P. A. Anfinrud, Proc. Natl. Acad. Sci. U.S.A. 90, S801 (1993).
14. G. D. Goodno, A. Astinov, R. J. D. Miller, J. Phys. Chem. A 103, 10630 (1999).
15. G. S. Kachalova, A. N. Popov, H. D. Bartunik, Science 284, 473 (1999).
16. J. Vojtechovsky, K. Chu, J. Berendzen, R. M. Sweet, I. Schlichting, Biophys. J. 77, 2153 (1999).
17. R. F. Tilton Jr., I. D. Kuntz Jr., G. A. Petsko, Biochemistry 23, 2849 (1984).
18. E. E. Scott, Q. H. Gibson, J. S. Olson, J. Biol. Chem. 276, 5177 (2001).
19. V. Srajer et al., Biochemistry 40, 13802 (2001).
20. A. Ostermann, R. Waschipky, F. G. Parak, G. U. Nienhaus, Nature 404, 205 (2000).
21. M. Brunori et al., Proc. Natl. Acad. Sci. U.S.A. 97, 2058 (2000).
22. K. Chu et al., Nature 403, 921 (2000).
23. H. Frauenfelder, G. U. Nienhaus, J. B. Johnson, Ber. Bunsen-Ges. Phys. Chem. 95, 272 (1991).
24. A. Cho, Science 296, 1008 (2002).
25. We thank W. Eaton and G. Hummer for helpful comments, and D. Bourgeois for sharing his expertise in the analysis of Laue diffraction data. We are grateful to K. Moffat and V. Šrajer for their assistance during our early struggles to realize picosecond x-ray crystallography. This work was supported by grants from the Robert A. Welch Foundation (C-612), the NIH (HL47020 and GM35649), and the W. M. Keck Center for Computational Biology to J.O.; by grants from the Robert A. Welch Foundation (C-1142) and the NIH (AR40252) to G.P.; and by grants from the Korea Science and Engineering Foundation, through the Center for Integrated Molecular Systems (POSTECH), to M.L.