1s8g

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[[Image:1s8g.jpg|left|200px]]<br /><applet load="1s8g" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1s8g.jpg|left|200px]]
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caption="1s8g, resolution 2.30&Aring;" />
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'''Crystal structure of Lys49-Phospholipase A2 from Agkistrodon contortrix laticinctus, fatty acid bound form'''<br />
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{{Structure
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|PDB= 1s8g |SIZE=350|CAPTION= <scene name='initialview01'>1s8g</scene>, resolution 2.30&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=DAO:LAURIC+ACID'>DAO</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
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|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]
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|GENE=
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}}
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'''Crystal structure of Lys49-Phospholipase A2 from Agkistrodon contortrix laticinctus, fatty acid bound form'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1S8G is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Agkistrodon_contortrix_laticinctus Agkistrodon contortrix laticinctus] with <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=DAO:'>DAO</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S8G OCA].
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1S8G is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Agkistrodon_contortrix_laticinctus Agkistrodon contortrix laticinctus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S8G OCA].
==Reference==
==Reference==
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A molecular mechanism for Lys49-phospholipase A2 activity based on ligand-induced conformational change., Ambrosio AL, Nonato MC, de Araujo HS, Arni R, Ward RJ, Ownby CL, de Souza DH, Garratt RC, J Biol Chem. 2005 Feb 25;280(8):7326-35. Epub 2004 Dec 13. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15596433 15596433]
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A molecular mechanism for Lys49-phospholipase A2 activity based on ligand-induced conformational change., Ambrosio AL, Nonato MC, de Araujo HS, Arni R, Ward RJ, Ownby CL, de Souza DH, Garratt RC, J Biol Chem. 2005 Feb 25;280(8):7326-35. Epub 2004 Dec 13. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15596433 15596433]
[[Category: Agkistrodon contortrix laticinctus]]
[[Category: Agkistrodon contortrix laticinctus]]
[[Category: Phospholipase A(2)]]
[[Category: Phospholipase A(2)]]
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[[Category: snake venom]]
[[Category: snake venom]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:59:10 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:01:49 2008''

Revision as of 12:01, 20 March 2008


PDB ID 1s8g

Drag the structure with the mouse to rotate
, resolution 2.30Å
Ligands: , and
Activity: Phospholipase A(2), with EC number 3.1.1.4
Coordinates: save as pdb, mmCIF, xml



Crystal structure of Lys49-Phospholipase A2 from Agkistrodon contortrix laticinctus, fatty acid bound form


Overview

Agkistrodon contortrix laticinctus myotoxin is a Lys(49)-phospholipase A(2) (EC 3.1.1.4) isolated from the venom of the serpent A. contortrix laticinctus (broad-banded copperhead). We present here three monomeric crystal structures of the myotoxin, obtained under different crystallization conditions. The three forms present notable structural differences and reveal that the presence of a ligand in the active site (naturally presumed to be a fatty acid) induces the exposure of a hydrophobic surface (the hydrophobic knuckle) toward the C terminus. The knuckle in A. contortrix laticinctus myotoxin involves the side chains of Phe(121) and Phe(124) and is a consequence of the formation of a canonical structure for the main chain within the region of residues 118-125. Comparison with other Lys(49)-phospholipase A(2) myotoxins shows that although the knuckle is a generic structural motif common to all members of the family, it is not readily recognizable by simple sequence analyses. An activation mechanism is proposed that relates fatty acid retention at the active site to conformational changes within the C-terminal region, a part of the molecule that has long been associated with Ca(2+)-independent membrane damaging activity and myotoxicity. This provides, for the first time, a direct structural connection between the phospholipase "active site" and the C-terminal "myotoxic site," justifying the otherwise enigmatic conservation of the residues of the former in supposedly catalytically inactive molecules.

About this Structure

1S8G is a Single protein structure of sequence from Agkistrodon contortrix laticinctus. Full crystallographic information is available from OCA.

Reference

A molecular mechanism for Lys49-phospholipase A2 activity based on ligand-induced conformational change., Ambrosio AL, Nonato MC, de Araujo HS, Arni R, Ward RJ, Ownby CL, de Souza DH, Garratt RC, J Biol Chem. 2005 Feb 25;280(8):7326-35. Epub 2004 Dec 13. PMID:15596433

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