2b96
From Proteopedia
(New page: 200px<br /><applet load="2b96" size="450" color="white" frame="true" align="right" spinBox="true" caption="2b96, resolution 1.70Å" /> '''Third Calcium ion fo...) |
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| - | [[Image:2b96.gif|left|200px]]<br /><applet load="2b96" size=" | + | [[Image:2b96.gif|left|200px]]<br /><applet load="2b96" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2b96, resolution 1.70Å" /> | caption="2b96, resolution 1.70Å" /> | ||
'''Third Calcium ion found in an inhibitor bound phospholipase A2'''<br /> | '''Third Calcium ion found in an inhibitor bound phospholipase A2'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The lipolytic enzyme phospholipase A2 plays a crucial role in lipid | + | The lipolytic enzyme phospholipase A2 plays a crucial role in lipid metabolism and catalyzes hydrolysis of the fatty-acid ester bond at the sn-2 position of phospholipids. Here, the crystal structure (1.7 A resolution) of the triple mutant (K53,56,121M) of bovine pancreatic phospholipase A2 complexed with an organic molecule, p-methoxybenzoic acid (anisic acid), is reported. Residues 60-70 (the surface-loop residues) are ordered and adopt conformations which are different from those normally found in structures in which a second calcium ion is present. It is interesting to note that for the first time a third calcium ion has been identified. In addition, four Tris (2-amino-2-hydroxymethyl-1,3-propanediol) molecules were located. It is believed that one of the Tris molecules plays a role in clamping the third calcium ion and that another is involved in controlling the dynamics of the surface loop through hydrogen bonds. |
==About this Structure== | ==About this Structure== | ||
| - | 2B96 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with CA, CL, TRS and ANN 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:// | + | 2B96 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=TRS:'>TRS</scene> and <scene name='pdbligand=ANN:'>ANN</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=2B96 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Sekar, K.]] | [[Category: Sekar, K.]] | ||
| - | [[Category: Tsai, M | + | [[Category: Tsai, M D.]] |
[[Category: Velmurugan, D.]] | [[Category: Velmurugan, D.]] | ||
[[Category: Yamane, T.]] | [[Category: Yamane, T.]] | ||
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[[Category: triple mutant]] | [[Category: triple mutant]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:35:23 2008'' |
Revision as of 14:35, 21 February 2008
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Third Calcium ion found in an inhibitor bound phospholipase A2
Overview
The lipolytic enzyme phospholipase A2 plays a crucial role in lipid metabolism and catalyzes hydrolysis of the fatty-acid ester bond at the sn-2 position of phospholipids. Here, the crystal structure (1.7 A resolution) of the triple mutant (K53,56,121M) of bovine pancreatic phospholipase A2 complexed with an organic molecule, p-methoxybenzoic acid (anisic acid), is reported. Residues 60-70 (the surface-loop residues) are ordered and adopt conformations which are different from those normally found in structures in which a second calcium ion is present. It is interesting to note that for the first time a third calcium ion has been identified. In addition, four Tris (2-amino-2-hydroxymethyl-1,3-propanediol) molecules were located. It is believed that one of the Tris molecules plays a role in clamping the third calcium ion and that another is involved in controlling the dynamics of the surface loop through hydrogen bonds.
About this Structure
2B96 is a Single protein structure of sequence from Bos taurus with , , and as ligands. Active as Phospholipase A(2), with EC number 3.1.1.4 Full crystallographic information is available from OCA.
Reference
Third calcium ion found in an inhibitor-bound phospholipase A2., Sekar K, Gayathri D, Velmurugan D, Jeyakanthan J, Yamane T, Poi MJ, Tsai MD, Acta Crystallogr D Biol Crystallogr. 2006 Apr;62(Pt 4):392-7. Epub 2006, Mar 18. PMID:16552140
Page seeded by OCA on Thu Feb 21 16:35:23 2008
Categories: Bos taurus | Phospholipase A(2) | Single protein | Sekar, K. | Tsai, M D. | Velmurugan, D. | Yamane, T. | ANN | CA | CL | TRS | Alpha helix | Anisic acid | Beta sheet | Triple mutant
