2bax: Difference between revisions

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{{STRUCTURE_2bax|  PDB=2bax  |  SCENE=  }}  
{{STRUCTURE_2bax|  PDB=2bax  |  SCENE=  }}  


'''Atomic Resolution Structure of the Double Mutant (K53,56M) of Bovine Pancreatic Phospholipase A2'''
===Atomic Resolution Structure of the Double Mutant (K53,56M) of Bovine Pancreatic Phospholipase A2===




==Overview==
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The enzyme phospholipase A2 catalyzes the hydrolysis of the sn-2 acyl chain of phospholipids, forming fatty acids and lysophospholipids. The crystal structure of a triple mutant (K53,56,121M) of bovine pancreatic phospholipase A2 in which the lysine residues at positions 53, 56 and 121 are replaced recombinantly by methionines has been determined at atomic resolution (0.97 A). The crystal is monoclinic (space group P2), with unit-cell parameters a = 36.934, b = 23.863, c = 65.931 A, beta = 101.47 degrees. The structure was solved by molecular replacement and has been refined to a final R factor of 10.6% (Rfree = 13.4%) using 63,926 unique reflections. The final protein model consists of 123 amino-acid residues, two calcium ions, one chloride ion, 243 water molecules and six 2-methyl-2,4-pentanediol molecules. The surface-loop residues 60-70 are ordered and have clear electron density.
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==About this Structure==
==About this Structure==
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==Reference==
==Reference==
Atomic resolution (0.97 A) structure of the triple mutant (K53,56,121M) of bovine pancreatic phospholipase A2., Sekar K, Rajakannan V, Gayathri D, Velmurugan D, Poi MJ, Dauter M, Dauter Z, Tsai MD, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Jan 1;61(Pt 1):3-7., Epub 2004 Sep 25. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16508077 16508077]
Atomic resolution (0.97 A) structure of the triple mutant (K53,56,121M) of bovine pancreatic phospholipase A2., Sekar K, Rajakannan V, Gayathri D, Velmurugan D, Poi MJ, Dauter M, Dauter Z, Tsai MD, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Jan 1;61(Pt 1):3-7., Epub 2004 Sep 25. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16508077 16508077]
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: Phospholipase a2]]
[[Category: Phospholipase a2]]
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