Crystal structure of pentalenene synthase: Mechanistic insights on terpenoid cyclization reactions in biology

Science

Volumn 277, Issue 5333, 1997, Pages 1820-1824

  Lesburg, Charles A ^a   Zhai, Guangzhi ^a   Cane, David E ^a   Christianson, David W ^a  

^a NONE

Author keywords

[No Author keywords available]

Indexed keywords

TERPENOID;

ARTICLE; BIODIVERSITY; CATALYSIS; CRYSTAL STRUCTURE; CYCLIZATION; ENZYME ACTIVE SITE; MULTIGENE FAMILY; PRIORITY JOURNAL; STEM CELL;

ALKYL AND ARYL TRANSFERASES; BINDING SITES; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; CYCLIZATION; CYCLOPENTANES; GERANYLTRANSTRANSFERASE; INTRAMOLECULAR LYASES; ISOMERASES; MODELS, MOLECULAR; POLYISOPRENYL PHOSPHATES; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS; STREPTOMYCES; TRANSFERASES;

EID: 0030777210     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.277.5333.1820     Document Type: Article

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44. Figures 1 and 2 were prepared with (i) MOLSCRIPT: P. Kraulis, J. Appl. Crystallogr. 24, 946 (1991); and (ii) Raster3D: D. J. Bacon and W. F. Anderson, J. Mol. Graph. 6, 219 (1988); E. A. Merritt and M. E. P. Murphy, Acta Crystallogr. D50, 869 (1994).
45. Figures 1 and 2 were prepared with (i) MOLSCRIPT: P. Kraulis, J. Appl. Crystallogr. 24, 946 (1991); and (ii) Raster3D: D. J. Bacon and W. F. Anderson, J. Mol. Graph. 6, 219 (1988); E. A. Merritt and M. E. P. Murphy, Acta Crystallogr. D50, 869 (1994).
46. We thank G. Farber, A. Jain, Z. Kanyo, W. N. Lipscomb, M. D. Lloyd, P. Lu, P. Sprengler, T. Stams, and G. M. Whitesides for helpful discussions during the course of this investigation and J. Noel for sharing data on the structure of epi-aristolochene synthase prior to publication. Supported by grants from the National Institutes of Health. This work is based upon research conducted at the Cornell High Energy Synchrotron Source (CHESS), which is supported by the National Science Foundation under award DMR-9311772, with the use of the Macromolecular Diffraction at CHESS (MacCHESS) facility, which is supported by award RR-01646 from the National Institutes of Health. Atomic coordinates have been deposited in the Brookhaven Protein Data Bank with accession code 1PS1.