2b96: Difference between revisions

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[[Image:2b96.gif|left|200px]]
{{Seed}}
[[Image:2b96.png|left|200px]]


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{{STRUCTURE_2b96|  PDB=2b96  |  SCENE=  }}  
{{STRUCTURE_2b96|  PDB=2b96  |  SCENE=  }}  


'''Third Calcium ion found in an inhibitor bound phospholipase A2'''
===Third Calcium ion found in an inhibitor bound phospholipase A2===




==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 16552140 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16552140}}


==About this Structure==
==About this Structure==
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==Reference==
==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:[http://www.ncbi.nlm.nih.gov/pubmed/16552140 16552140]
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:[http://www.ncbi.nlm.nih.gov/pubmed/16552140 16552140]
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]
Observation of additional calcium ion in the crystal structure of the triple mutant K56,120,121M of bovine pancreatic phospholipase A2., Rajakannan V, Yogavel M, Poi MJ, Jeyaprakash AA, Jeyakanthan J, Velmurugan D, Tsai MD, Sekar K, J Mol Biol. 2002 Dec 6;324(4):755-62. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12460575 12460575]
High-resolution refinement of orthorhombic bovine pancreatic phospholipase A2., Sekar K, Sundaralingam M, Acta Crystallogr D Biol Crystallogr. 1999 Jan;55(Pt 1):46-50. Epub 1999, Jan 1. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10089393 10089393]
Phospholipase A2 engineering. Structural and functional roles of the highly conserved active site residue aspartate-99., Sekar K, Yu BZ, Rogers J, Lutton J, Liu X, Chen X, Tsai MD, Jain MK, Sundaralingam M, Biochemistry. 1997 Mar 18;36(11):3104-14. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9115986 9115986]
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Beta sheet]]
[[Category: Beta sheet]]
[[Category: Triple mutant]]
[[Category: Triple mutant]]
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