2ph4
From Proteopedia
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'''Crystal structure of a novel Arg49 phospholipase A2 homologue from Zhaoermia mangshanensis venom''' | '''Crystal structure of a novel Arg49 phospholipase A2 homologue from Zhaoermia mangshanensis venom''' | ||
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[[Category: Mebs, D.]] | [[Category: Mebs, D.]] | ||
[[Category: Murakami, M T.]] | [[Category: Murakami, M T.]] | ||
| - | [[Category: | + | [[Category: Arg49]] |
| - | [[Category: | + | [[Category: Myotoxin]] |
| - | [[Category: | + | [[Category: Phospholipase a2]] |
| - | [[Category: | + | [[Category: Snake venom]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr 16 23:07:22 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 20:07, 16 April 2008
Crystal structure of a novel Arg49 phospholipase A2 homologue from Zhaoermia mangshanensis venom
Overview
The venom of Zhaoermia mangshanensis, encountered solely in Mt Mang in China's Hunan Province, exhibits coagulant, phosphodiesterase, l-amino acid oxidase, kallikrein, phospholipase A(2) and myotoxic activities. The catalytically inactive PLA(2) homolog referred to as zhaoermiatoxin is highly myotoxic and displays high myonecrotic and edema activities. Zhaoermiatoxin possesses a molecular weight of 13,972Da, consists of 121 amino-acid residues cross-linked by seven disulfide bridges and shares high sequence homology with Lys49-PLA(2)s from the distantly related Asian pitvipers. However, zhaoermiatoxin possesses an arginine residue at position 49 instead of a lysine, thereby suggesting a secondary Lys49-->Arg substitution which results in a catalytically inactive protein. We have determined the first crystal structure of zhaoermiatoxin, an Arg49-PLA(2), from Zhaoermia mangshanensis venom at 2.05A resolution, which represents a novel member of phospholipase A(2) family. In this structure, unlike the Lys49 PLA(2)s, the C-terminus is well ordered and an unexpected non-polarized state of the putative calcium-binding loop due to the flip of Lys122 towards the bulk solvent is observed. The orientation of the Arg-49 side chain results in a similar binding mode to that observed in the Lys49 PLA(2)s; however, the guadinidium group is tri-coordinated by carbonyl oxygen atoms of the putative calcium-binding loop, whereas the Nzeta atom of lysine is tetra-coordinated as a result of the different conformation adopted by the putative calcium-binding loop.
About this Structure
2PH4 is a Single protein structure of sequence from Zhaoermia mangshanensis. Full crystallographic information is available from OCA.
Reference
Crystal structure of a novel myotoxic Arg49 phospholipase A(2) homolog (zhaoermiatoxin) from Zhaoermia mangshanensis snake venom: Insights into Arg49 coordination and the role of Lys122 in the polarization of the C-terminus., Murakami MT, Kuch U, Betzel C, Mebs D, Arni RK, Toxicon. 2008 Apr;51(5):723-35. Epub 2007 Nov 29. PMID:18295812 Page seeded by OCA on Wed Apr 16 23:07:22 2008
