Abstract
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 to 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.
Original language | English (US) |
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Pages (from-to) | 1563-1566 |
Number of pages | 4 |
Journal | Science |
Volume | 250 |
Issue number | 4987 |
State | Published - Dec 14 1990 |
ASJC Scopus subject areas
- General