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

David L. Scott, Zbyszek Otwinowski, Michael H. Gelb, Paul B. Sigler

Research output: Contribution to journalArticle

296 Citations (Scopus)

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 languageEnglish (US)
Pages (from-to)1563-1566
Number of pages4
JournalScience
Volume250
Issue number4987
StatePublished - Dec 14 1990

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Bee Venoms
Phospholipases A2
Organophosphonates
Phospholipases
Enzymes
Carbohydrates
Electrons

ASJC Scopus subject areas

  • General

Cite this

Crystal structure of bee-venom phospholipase A2 in a complex with a transition-state analogue. / Scott, David L.; Otwinowski, Zbyszek; Gelb, Michael H.; Sigler, Paul B.

In: Science, Vol. 250, No. 4987, 14.12.1990, p. 1563-1566.

Research output: Contribution to journalArticle

Scott, DL, Otwinowski, Z, Gelb, MH & Sigler, PB 1990, 'Crystal structure of bee-venom phospholipase A2 in a complex with a transition-state analogue', Science, vol. 250, no. 4987, pp. 1563-1566.
Scott, David L. ; Otwinowski, Zbyszek ; Gelb, Michael H. ; Sigler, Paul B. / Crystal structure of bee-venom phospholipase A2 in a complex with a transition-state analogue. In: Science. 1990 ; Vol. 250, No. 4987. pp. 1563-1566.
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