1psj: Difference between revisions

New page: left|200px<br /><applet load="1psj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1psj, resolution 2.0Å" /> '''ACIDIC PHOSPHOLIPASE ...
 
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[[Image:1psj.gif|left|200px]]<br /><applet load="1psj" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1psj.gif|left|200px]]<br /><applet load="1psj" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1psj, resolution 2.0&Aring;" />
caption="1psj, resolution 2.0&Aring;" />
'''ACIDIC PHOSPHOLIPASE A2 FROM AGKISTRODON HALYS PALLAS'''<br />
'''ACIDIC PHOSPHOLIPASE A2 FROM AGKISTRODON HALYS PALLAS'''<br />


==Overview==
==Overview==
The crystal structure of acidic phospholipase A2 from the venom of, Agkistrodon halys pallas has been determined by molecular replacement at, 2.0 A resolution to a crystallographic R-factor of 0.157. The overall, structure of the molecule is very similar to those of other phospholipase, A2 species of known structure. The catalytic site, the hydrophobic channel, and the N-terminal region show greatest structural conservation. The, Ca(2+)-binding region has a conformation that resembles closely that of, bovine PLA2 rather than Crotalus atrox PLA2. Compared with other PLA2, species, the conformation of the C-terminal ridge shows significant, difference due to the insertion of two residues. A unique aromatic patch, appears on one face of the molecules, surrounded by two acidic residues, the relevant features of this structure and their possible biological, implications are discussed.
The crystal structure of acidic phospholipase A2 from the venom of Agkistrodon halys pallas has been determined by molecular replacement at 2.0 A resolution to a crystallographic R-factor of 0.157. The overall structure of the molecule is very similar to those of other phospholipase A2 species of known structure. The catalytic site, the hydrophobic channel and the N-terminal region show greatest structural conservation. The Ca(2+)-binding region has a conformation that resembles closely that of bovine PLA2 rather than Crotalus atrox PLA2. Compared with other PLA2 species, the conformation of the C-terminal ridge shows significant difference due to the insertion of two residues. A unique aromatic patch appears on one face of the molecules, surrounded by two acidic residues, the relevant features of this structure and their possible biological implications are discussed.


==About this Structure==
==About this Structure==
1PSJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gloydius_halys Gloydius halys] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PSJ OCA].  
1PSJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gloydius_halys Gloydius halys] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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=1PSJ OCA].  


==Reference==
==Reference==
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[[Category: Phospholipase A(2)]]
[[Category: Phospholipase A(2)]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Lin, Z.J.]]
[[Category: Lin, Z J.]]
[[Category: Wang, X.Q.]]
[[Category: Wang, X Q.]]
[[Category: CA]]
[[Category: CA]]
[[Category: calcium]]
[[Category: calcium]]
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[[Category: lipid degradation]]
[[Category: lipid degradation]]


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