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Science 14 December 1990:
Vol. 250. no. 4987, pp. 1560 - 1563
DOI: 10.1126/science.2274787
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Articles
Science, Vol 250, Issue 4987, 1560-1563
Copyright © 1990 by American Association for the Advancement of Science
Crystal structure of cobra-venom phospholipase A2 in a complex with a transition-state analogue
SP White,
DL Scott,
Z Otwinowski,
MH Gelb,
and
PB Sigler
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06511.
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.
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