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

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

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Abstract

The crystal structure of a complex between a phosphonate transition-state analogue and the phospholipase A2 (PLA2) from Naja naja atra venom has been solved and refined to a resolution of 2.0 angstroms. The identical stereochemistry of the two complexes that comprise the crystal's asymmetric unit indicates both the manner in which the transition state is stabilized and how the Hydrophobic fatty acyl chains of the substrate are accommodated by the enzyme during interfacial catalysis. The critical features that suggest the chemistry of binding and catalysis are the same as those seen in the crystal structure of a similar complex formed with the evolutionarily distant bee-venom PLA2.

Original languageEnglish (US)
Pages (from-to)1560-1563
Number of pages4
JournalScience
Volume250
Issue number4987
Publication statusPublished - Dec 14 1990

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Cite this

White, S. P., Scott, D. L., Otwinowski, Z., Gelb, M. H., & Sigler, P. B. (1990). Crystal structure of cobra-venom phospholipase A2 in a complex with a transition-state analogue. Science, 250(4987), 1560-1563.