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Science 14 December 1990:
Vol. 250. no. 4987, pp. 1563 - 1566
DOI: 10.1126/science.2274788
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Articles

Science, Vol 250, Issue 4987, 1563-1566
Copyright © 1990 by American Association for the Advancement of Science

articles

Crystal structure of bee-venom phospholipase A2 in a complex with a transition-state analogue

DL Scott, Z Otwinowski, MH Gelb, and PB Sigler

Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06511.

The 2.0 angstroms crystal structure of a complex containing bee-venom phospholipase A2 (PLA2) and a phosphonate transition-state analogue was solved by multiple isomorphous replacement. The electron-density map is sufficiently detailed to visualize the proximal sugars of the enzyme's N-linked carbohydrate and a single molecule of the transition-state analogue bound ot its active center. Although bee-venom PLA2 does not belong to the large homologous Class I/II family that encompasses most other well-studied PLA2s, there is segmental sequence similarity and conservation of many functional substructures. Comparison of the bee-venom enzyme with other phospholipase structures provides compelling evidence for a common catalytic mechanism.


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Science. ISSN 0036-8075 (print), 1095-9203 (online)