1poc
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(New page: 200px<br /><applet load="1poc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1poc, resolution 2.0Å" /> '''CRYSTAL STRUCTURE OF ...)
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Revision as of 21:51, 20 November 2007
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CRYSTAL STRUCTURE OF BEE-VENOM PHOSPHOLIPASE A2 IN A COMPLEX WITH A TRANSITION-STATE ANALOGUE
Overview
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 ot 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.
About this Structure
1POC is a Single protein structure of sequence from Apis mellifera with CA and GEL as ligands. Active as Phospholipase A(2), with EC number 3.1.1.4 Full crystallographic information is available from OCA.
Reference
Crystal structure of bee-venom phospholipase A2 in a complex with a transition-state analogue., Scott DL, Otwinowski Z, Gelb MH, Sigler PB, Science. 1990 Dec 14;250(4987):1563-6. PMID:2274788
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