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1god
From Proteopedia
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(New page: 200px<br /><applet load="1god" size="450" color="white" frame="true" align="right" spinBox="true" caption="1god, resolution 2.8Å" /> '''MONOMERIC LYS-49 PHOS...)
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Revision as of 14:04, 20 November 2007
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MONOMERIC LYS-49 PHOSPHOLIPASE A2 HOMOLOGUE ISOLATED FROM THE VENOM OF CERROPHIDION (BOTHROPS) GODMANI
Overview
Lys49-Phospholipase A2 (Lys49-PLA2) homologues damage membranes by a, Ca2+-independent mechanism which does not involve catalytic activity. With, the aim of determining the structural basis for this novel activity, we, have solved the crystal structure of myotoxin-II, a Lys49-PLA2 isolated, from the venom of Cerrophidion (Bothrops) godmani (godMT-II) at 2.8 A, resolution by molecular replacement. The final model has been refined to a, final crystallografic residual (Rfactor) of 18.8% (Rfree = 28.2%), with, excellent stereochemistry. godMT-II is also monomeric in the crystalline, state, and small-angle X-ray scattering results demonstrate that the, protein is monomeric in solution under fisicochemical conditions similar, to those used in the crystallographic studies.
About this Structure
1GOD is a Single protein structure of sequence from Cerrophidion godmani. Active as Phospholipase A(2), with EC number 3.1.1.4 Full crystallographic information is available from OCA.
Reference
Crystal structure of myotoxin II, a monomeric Lys49-phospholipase A2 homologue isolated from the venom of Cerrophidion (Bothrops) godmani., Arni RK, Fontes MR, Barberato C, Gutierrez JM, Diaz C, Ward RJ, Arch Biochem Biophys. 1999 Jun 15;366(2):177-82. PMID:10356281
Page seeded by OCA on Tue Nov 20 16:12:07 2007
