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Science 6 August 1993:
Vol. 261. no. 5122, pp. 731 - 736
DOI: 10.1126/science.8342039
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Articles

Science, Vol 261, Issue 5122, 731-736
Copyright © 1993 by American Association for the Advancement of Science

articles

Crystal structure of hemoprotein domain of P450BM-3, a prototype for microsomal P450's

KG Ravichandran, SS Boddupalli, CA Hasermann, JA Peterson, and J Deisenhofer

Howard Hughes Medical Institute, University of Texas Southwestern Medical Center, Dallas 75235-9050.

Cytochrome P450BM-3, a bacterial fatty acid monoxygenase, resembles the eukaryotic microsomal P450's and their flavoprotein reductase in primary structure and function. The three-dimensional structure of the hemoprotein domain of P450BM-3 was determined by x-ray diffraction and refined to an R factor of 16.9 percent at 2.0 angstrom resolution. The structure consists of an alph and a beta domain. The active site heme is accessible through a long hydrophobic channel formed primarily by the beta domain and the B' and F helices of the alpha domain. The two molecules in the asymmetric unit differ in conformation around the substrate binding pocket. Substantial differences between P450BM-3 and P450cam, the only other P450 structure available, are observed around the substrate binding pocket and the regions important for redox partner binding. A general mechanism for proton transfer in P450's is also proposed.


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E. A. Dierks, Z. Zhang, E. F. Johnson, and P. R. O. de Montellano (1998)
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A. Nikoshkov, S. Lajic, A. Vlamis-Gardikas, L. Tranebjarg, M. Holst, A. Wedell, and H. Luthman (1998)
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   Abstract »    Full Text »    PDF »
Characterization of Inducible Nitric-oxide Synthase by Cytochrome P-450 Substrates and Inhibitors. INHIBITION BY CHLORZOXAZONE.
S. K. Grant, B. G. Green, R. Wang, S. G. Pacholok, and J. W. Kozarich (1997)
J. Biol. Chem. 272, 977-983
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Synergistic Effect of Partially Inactivating Mutations in Steroid 21-Hydroxylase Deficiency.
A. Nikoshkov, S. Lajic, M. Holst, A. Wedell, and H. Luthman (1997)
J. Clin. Endocrinol. Metab. 82, 194-199
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Inherited Forms of Mineralocorticoid Hypertension.
P. C. White (1996)
Hypertension 28, 927-936
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Molecular Engineering Study on Electron Transfer from NADPH-P450 Reductase to Rat Mitochondrial P450c27 in Yeast Microsomes.
T. Sakaki, S. Kominami, K. Hayashi, M. Akiyoshi-Shibata, and Y. Yabusaki (1996)
J. Biol. Chem. 271, 26209-26213
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Putidaredoxin Reductase-Putidaredoxin-Cytochrome P450cam Triple Fusion Protein. CONSTRUCTION OF A SELF-SUFFICIENT ESCHERICHIA COLI CATALYTIC SYSTEM.
O. Sibbesen, J. J. De Voss, and P. R.O. d. Montellano (1996)
J. Biol. Chem. 271, 22462-22469
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The Highly Stereoselective Oxidation of Polyunsaturated Fatty Acids by Cytochrome P450BM-3.
J. H. Capdevila, S. Wei, C. Helvig, J. R. Falck, Y. Belosludtsev, G. Truan, S. E. Graham-Lorence, and J. A. Peterson (1996)
J. Biol. Chem. 271, 22663-22671
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Identification of Thromboxane A2 Synthase Active Site Residues by Molecular Modeling-guided Site-directed Mutagenesis.
L.-H. Wang, N. Matijevic-Aleksic, P.-Y. Hsu, K.-H. Ruan, K. K. Wu, and R. J. Kulmacz (1996)
J. Biol. Chem. 271, 19970-19975
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Conserved Glu[IMAGE] at the Cytochrome P450 1A2 Distal Site Is Crucial in the Nitric Oxide Complex Stability.
R. Nakano, H. Sato, A. Watanabe, O. Ito, and T. Shimizu (1996)
J. Biol. Chem. 271, 8570-8574
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Engineering a Mineralocorticoid- to a Glucocorticoid-synthesizing Cytochrome P450.
B. Böttner, H. Schrauber, and R. Bernhardt (1996)
J. Biol. Chem. 271, 8028-8033
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Evidence That Aspartic Acid 301 Is a Critical Substrate-Contact Residue in the Active Site of Cytochrome P450 2D6.
S. W. Ellis, G. P. Hayhurst, G. Smith, T. Lightfoot, M. M. S. Wong, A. P. Simula, M. J. Ackland, M. J. E. Sternberg, M. S. Lennard, G. T. Tucker, et al. (1995)
J. Biol. Chem. 270, 29055-29058
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The Stoichiometry of the Cytochrome P-450-catalyzed Metabolism of Methoxyflurane and Benzphetamine in the Presence and Absence of Cytochrome b(5).
L. D. Gruenke, K. Konopka, M. Cadieu, and L. Waskell (1995)
J. Biol. Chem. 270, 24707-24718
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