1vl9

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(New page: 200px<br /><applet load="1vl9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1vl9, resolution 0.97&Aring;" /> '''Atomic resolution (0...)
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[[Image:1vl9.gif|left|200px]]<br /><applet load="1vl9" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1vl9.gif|left|200px]]<br /><applet load="1vl9" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1vl9, resolution 0.97&Aring;" />
caption="1vl9, resolution 0.97&Aring;" />
'''Atomic resolution (0.97A) structure of the triple mutant (K53,56,121M) of bovine pancreatic phospholipase A2'''<br />
'''Atomic resolution (0.97A) structure of the triple mutant (K53,56,121M) of bovine pancreatic phospholipase A2'''<br />
==Overview==
==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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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.
==About this Structure==
==About this Structure==
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1VL9 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, MRD and MPD 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1VL9 OCA].
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1VL9 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=MRD:'>MRD</scene> and <scene name='pdbligand=MPD:'>MPD</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=1VL9 OCA].
==Reference==
==Reference==
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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 Crystallograph Sect F Struct Biol Cryst Commun. 2005 Jan 1;61(Pt, 1):3-7. Epub 2004 Sep 25. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16508077 16508077]
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=16508077 16508077]
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Phospholipase A(2)]]
[[Category: Phospholipase A(2)]]
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[[Category: Dauter, Z.]]
[[Category: Dauter, Z.]]
[[Category: Gayathri, D.]]
[[Category: Gayathri, D.]]
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[[Category: Poi, M.J.]]
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[[Category: Poi, M J.]]
[[Category: Rajakannan, V.]]
[[Category: Rajakannan, V.]]
[[Category: Sekar, K.]]
[[Category: Sekar, K.]]
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[[Category: Tsai, M.D.]]
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[[Category: Tsai, M D.]]
[[Category: Velmurugan, D.]]
[[Category: Velmurugan, D.]]
[[Category: CA]]
[[Category: CA]]
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[[Category: triple mutant]]
[[Category: triple mutant]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 04:55:51 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:36:39 2008''

Revision as of 13:36, 21 February 2008


1vl9, resolution 0.97Å

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Atomic resolution (0.97A) structure of the triple mutant (K53,56,121M) of bovine pancreatic phospholipase A2

Overview

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.

About this Structure

1VL9 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

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:16508077

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