1e1a
From Proteopedia
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Revision as of 12:59, 30 October 2007
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CRYSTAL STRUCTURE OF DFPASE FROM LOLIGO VULGARIS
Overview
BACKGROUND: Phosphotriesterases (PTE) are enzymes capable of detoxifying, organophosphate-based chemical warfare agents by hydrolysis. One subclass, of these enzymes comprises the family of diisopropylfluorophosphatases, (DFPases). The DFPase reported here was originally isolated from squid, head ganglion of Loligo vulgaris and can be characterized as squid-type, DFPase. It is capable of hydrolyzing the organophosphates, diisopropylfluorophosphate, soman, sarin, tabun, and cyclosarin. RESULTS:, Crystals were grown of both the native and the selenomethionine-labeled, enzyme. The X-ray crystal structure of the DFPase from Loligo vulgaris has, been solved by MAD phasing and refined to a crystallographic R value of, 17.6% at a final resolution of 1.8 A. Using site-directed mutagenesis, we, ... [(full description)]
About this Structure
1E1A is a [Single protein] structure of sequence from [Loligo vulgaris] with CA as [ligand]. Active as [Diisopropyl-fluorophosphatase], with EC number [3.1.8.2]. Structure known Active Site: DFP. Full crystallographic information is available from [OCA].
Reference
Crystal structure of diisopropylfluorophosphatase from Loligo vulgaris., Scharff EI, Koepke J, Fritzsch G, Lucke C, Ruterjans H, Structure. 2001 Jun;9(6):493-502. PMID:11435114
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