1jlt
From Proteopedia
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|PDB= 1jlt |SIZE=350|CAPTION= <scene name='initialview01'>1jlt</scene>, resolution 1.4Å | |PDB= 1jlt |SIZE=350|CAPTION= <scene name='initialview01'>1jlt</scene>, resolution 1.4Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Phospholipase_A(2) Phospholipase A(2)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.4 3.1.1.4] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Phospholipase_A(2) Phospholipase A(2)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.4 3.1.1.4] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1aok|1AOK]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jlt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jlt OCA], [http://www.ebi.ac.uk/pdbsum/1jlt PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1jlt RCSB]</span> | ||
}} | }} | ||
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[[Category: Rajashankar, K R.]] | [[Category: Rajashankar, K R.]] | ||
[[Category: Singh, T P.]] | [[Category: Singh, T P.]] | ||
| - | [[Category: MPD]] | ||
| - | [[Category: MRD]] | ||
[[Category: heterodimer complex]] | [[Category: heterodimer complex]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
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[[Category: vipoxin]] | [[Category: vipoxin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:35:35 2008'' |
Revision as of 18:35, 30 March 2008
| |||||||
| , resolution 1.4Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Activity: | Phospholipase A(2), with EC number 3.1.1.4 | ||||||
| Related: | 1AOK
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Vipoxin Complex
Overview
Vipoxin is a neurotoxic postsynaptic heterodimeric complex from the venom of Vipera ammodytes meridionalis, the most toxic snake in Europe. It consists of a basic and highly toxic phospholipase A(2) and an acidic non-toxic protein inhibitor. The two polypeptide chains have the same chain length and share 62% amino-acid identity. Vipoxin is a unique example of evolution of the catalytic and toxic phospholipase A(2) functions into inhibitory and non-toxic functions. The crystal structure of the complex has been determined by the molecular-replacement method and refined to 1.4 A resolution to an R factor of 18.2%. The complex formation decreases the accessible surface area of the two subunits by approximately 1480 A(2), which results in a reduction of toxicity and catalytic activity. The catalytic and substrate-binding sites of the vipoxin phospholipase A(2) are identical or similar to those of other group I/II enzymes. Two 2-methyl-2,4-pentanediol molecules are present in the hydrophobic channel close to the active site. The two subunits lack calcium ions. The negatively charged Asp49 of the phospholipase A(2), which participates in the Ca(2+)-binding sites of other snake-venom phospholipase A(2)s, is neutralized by the side chain of Lys69 from the inhibitor. Attempts have been made to identify the toxicity region and to explain the reduced catalytic activity and toxicity of the phospholipase A(2) subunit.
About this Structure
1JLT is a Protein complex structure of sequences from Vipera ammodytes ammodytes. Full crystallographic information is available from OCA.
Reference
Structure of the neurotoxic complex vipoxin at 1.4 A resolution., Banumathi S, Rajashankar KR, Notzel C, Aleksiev B, Singh TP, Genov N, Betzel C, Acta Crystallogr D Biol Crystallogr. 2001 Nov;57(Pt 11):1552-9. Epub 2001, Oct 25. PMID:11679719
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