2ph4: Difference between revisions
New page: left|200px {{Structure |PDB= 2ph4 |SIZE=350|CAPTION= <scene name='initialview01'>2ph4</scene>, resolution 2.05Å |SITE= <scene name='pdbsite=AC1:So4+Binding+Site+... |
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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''' | ||
==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== | ==About this Structure== | ||
2PH4 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Zhaoermia_mangshanensis Zhaoermia mangshanensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PH4 OCA]. | 2PH4 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Zhaoermia_mangshanensis Zhaoermia mangshanensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PH4 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:[http://www.ncbi.nlm.nih.gov/pubmed/18295812 18295812] | |||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Zhaoermia mangshanensis]] | [[Category: Zhaoermia mangshanensis]] | ||
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[[Category: snake venom]] | [[Category: snake venom]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 15:38:55 2008'' | ||
Revision as of 16:38, 23 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of a novel Arg49 phospholipase A2 homologue from Zhaoermia mangshanensis venom
OverviewOverview
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 StructureAbout this Structure
2PH4 is a Single protein structure of sequence from Zhaoermia mangshanensis. Full crystallographic information is available from OCA.
ReferenceReference
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
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