2ph4
From Proteopedia
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|PDB= 2ph4 |SIZE=350|CAPTION= <scene name='initialview01'>2ph4</scene>, resolution 2.05Å | |PDB= 2ph4 |SIZE=350|CAPTION= <scene name='initialview01'>2ph4</scene>, resolution 2.05Å | ||
|SITE= <scene name='pdbsite=AC1:So4+Binding+Site+For+Residue+A+301'>AC1</scene>, <scene name='pdbsite=AC2:So4+Binding+Site+For+Residue+A+302'>AC2</scene>, <scene name='pdbsite=AC3:So4+Binding+Site+For+Residue+B+303'>AC3</scene>, <scene name='pdbsite=AC4:So4+Binding+Site+For+Residue+B+304'>AC4</scene>, <scene name='pdbsite=AC5:So4+Binding+Site+For+Residue+B+305'>AC5</scene>, <scene name='pdbsite=AC6:Peg+Binding+Site+For+Residue+A+401'>AC6</scene> and <scene name='pdbsite=AC7:Peg+Binding+Site+For+Residue+B+402'>AC7</scene> | |SITE= <scene name='pdbsite=AC1:So4+Binding+Site+For+Residue+A+301'>AC1</scene>, <scene name='pdbsite=AC2:So4+Binding+Site+For+Residue+A+302'>AC2</scene>, <scene name='pdbsite=AC3:So4+Binding+Site+For+Residue+B+303'>AC3</scene>, <scene name='pdbsite=AC4:So4+Binding+Site+For+Residue+B+304'>AC4</scene>, <scene name='pdbsite=AC5:So4+Binding+Site+For+Residue+B+305'>AC5</scene>, <scene name='pdbsite=AC6:Peg+Binding+Site+For+Residue+A+401'>AC6</scene> and <scene name='pdbsite=AC7:Peg+Binding+Site+For+Residue+B+402'>AC7</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ph4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ph4 OCA], [http://www.ebi.ac.uk/pdbsum/2ph4 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ph4 RCSB]</span> | ||
}} | }} | ||
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[[Category: Mebs, D.]] | [[Category: Mebs, D.]] | ||
[[Category: Murakami, M T.]] | [[Category: Murakami, M T.]] | ||
| - | [[Category: PEG]] | ||
| - | [[Category: SO4]] | ||
[[Category: arg49]] | [[Category: arg49]] | ||
[[Category: myotoxin]] | [[Category: myotoxin]] | ||
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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 Mon Mar 31 04:35:53 2008'' |
Revision as of 01:35, 31 March 2008
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| , resolution 2.05Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , , , , , and | ||||||
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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