1o2e
From Proteopedia
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'''Structure of the triple mutant (K53,56,120M) + Anisic acid complex of phospholipase A2''' | '''Structure of the triple mutant (K53,56,120M) + Anisic acid complex of phospholipase A2''' | ||
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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:[http://www.ncbi.nlm.nih.gov/pubmed/14529623 14529623] | 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:[http://www.ncbi.nlm.nih.gov/pubmed/14529623 14529623] | ||
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
| - | [[Category: Phospholipase A(2)]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Sekar, K.]] | [[Category: Sekar, K.]] | ||
[[Category: Tsai, M D.]] | [[Category: Tsai, M D.]] | ||
[[Category: Velmurugan, D.]] | [[Category: Velmurugan, D.]] | ||
| - | [[Category: | + | [[Category: Alpha helix]] |
| - | [[Category: | + | [[Category: Anisic acid]] |
| - | [[Category: | + | [[Category: Beta sheet]] |
| - | [[Category: | + | [[Category: Triple mutant]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:16:07 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 00:16, 3 May 2008
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. 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 Sat May 3 03:16:07 2008
