Crystal Structure of Cobra-Venom Phospholipase A 2 in a Complex with a Transition-State Analogue
- 14 December 1990
- journal article
- research article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 250 (4987) , 1560-1563
- https://doi.org/10.1126/science.2274787
Abstract
The crystal structure of a complex between a phosphonate transition-state analogue and the phospholipase A 2 (PLA 2 ) 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 PLA 2 .This publication has 28 references indexed in Scilit:
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