1o2e
From Proteopedia
(New page: 200px<br /><applet load="1o2e" size="450" color="white" frame="true" align="right" spinBox="true" caption="1o2e, resolution 2.60Å" /> '''Structure of the tri...) |
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| - | [[Image:1o2e.jpg|left|200px]]<br /><applet load="1o2e" size=" | + | [[Image:1o2e.jpg|left|200px]]<br /><applet load="1o2e" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1o2e, resolution 2.60Å" /> | caption="1o2e, resolution 2.60Å" /> | ||
'''Structure of the triple mutant (K53,56,120M) + Anisic acid complex of phospholipase A2'''<br /> | '''Structure of the triple mutant (K53,56,120M) + Anisic acid complex of phospholipase A2'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Phospholipase A2 catalyses the hydrolysis of the ester bond of | + | Phospholipase A2 catalyses the hydrolysis of the ester bond of 3-sn-phosphoglycerides. Here, we report the crystal structures of the free and anisic acid-bound triple mutant (K53,56,120M) of bovine pancreatic phospholipase A2. In the bound triple mutant structure, the small organic molecule p-anisic acid is found in the active site, and one of the carboxylate oxygen atoms is coordinated to the functionally important primary calcium ion. The other carboxylate oxygen atom is hydrogen bonded to the phenolic hydroxyl group of Tyr69. In addition, the bound anisic acid molecule replaces one of the functionally important water molecules in the active site. The residues 60-70, which are in a loop (surface loop), are disordered in most of the bovine pancreatic phospholipase A2 structures. It is interesting to note that these residues are ordered in the bound triple mutant structure but are disordered in the free triple mutant structure. The organic crystallization ingredient 2-methyl-2,4-pentanediol is found near the active site of the free triple mutant structure. The overall tertiary folding and stereochemical parameters for the final models of the free and anisic acid-bound triple mutant are virtually identical. |
==About this Structure== | ==About this Structure== | ||
| - | 1O2E 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 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:// | + | 1O2E 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> 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=1O2E 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: ANN]] | [[Category: ANN]] | ||
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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 14:12:35 2008'' |
Revision as of 12:12, 21 February 2008
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Structure of the triple mutant (K53,56,120M) + Anisic acid complex of phospholipase A2
Overview
Phospholipase A2 catalyses the hydrolysis of the ester bond of 3-sn-phosphoglycerides. Here, we report the crystal structures of the free and anisic acid-bound triple mutant (K53,56,120M) of bovine pancreatic phospholipase A2. In the bound triple mutant structure, the small organic molecule p-anisic acid is found in the active site, and one of the carboxylate oxygen atoms is coordinated to the functionally important primary calcium ion. The other carboxylate oxygen atom is hydrogen bonded to the phenolic hydroxyl group of Tyr69. In addition, the bound anisic acid molecule replaces one of the functionally important water molecules in the active site. The residues 60-70, which are in a loop (surface loop), are disordered in most of the bovine pancreatic phospholipase A2 structures. It is interesting to note that these residues are ordered in the bound triple mutant structure but are disordered in the free triple mutant structure. The organic crystallization ingredient 2-methyl-2,4-pentanediol is found near the active site of the free triple mutant structure. The overall tertiary folding and stereochemical parameters for the final models of the free and anisic acid-bound triple mutant are virtually identical.
About this Structure
1O2E 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
Crystal structures of the free and anisic acid bound triple mutant of phospholipase A2., Sekar K, Vaijayanthi Mala S, Yogavel M, Velmurugan D, Poi MJ, Vishwanath BS, Gowda TV, Jeyaprakash AA, Tsai MD, J Mol Biol. 2003 Oct 17;333(2):367-76. PMID:14529623
Page seeded by OCA on Thu Feb 21 14:12:35 2008
Categories: Bos taurus | Phospholipase A(2) | Single protein | Sekar, K. | Tsai, M D. | Velmurugan, D. | ANN | CA | Alpha helix | Anisic acid | Beta sheet | Triple mutant
