1u73

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(New page: 200px<br /><applet load="1u73" size="450" color="white" frame="true" align="right" spinBox="true" caption="1u73, resolution 1.9&Aring;" /> '''Crystal structure of ...)
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[[Image:1u73.gif|left|200px]]<br /><applet load="1u73" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1u73, resolution 1.9&Aring;" />
caption="1u73, resolution 1.9&Aring;" />
'''Crystal structure of a Dimeric Acidic Platelet Aggregation Inhibitor and Hypotensive Phospholipase A2 from Bothrops jararacussu'''<br />
'''Crystal structure of a Dimeric Acidic Platelet Aggregation Inhibitor and Hypotensive Phospholipase A2 from Bothrops jararacussu'''<br />
==Overview==
==Overview==
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Phospholipases A2 belong to the superfamily of proteins which hydrolyzes, the sn-2 acyl groups of membrane phospholipids to release arachidonic acid, and lysophospholipids. An acidic phospholipase A2 isolated from Bothrops, jararacussu snake venom presents a high catalytic, platelet aggregation, inhibition and hypotensive activities. This protein was crystallized in, two oligomeric states: monomeric and dimeric. The crystal structures were, solved at 1.79 and 1.90 angstroms resolution, respectively, for the two, states. It was identified a Na+ ion at the center of Ca2+-binding site of, the monomeric form. A novel dimeric conformation with the active sites, exposed to the solvent was observed. Conformational states of the molecule, may be due to the physicochemical conditions used in the crystallization, experiments. We suggest dimeric state is one found in vivo.
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Phospholipases A2 belong to the superfamily of proteins which hydrolyzes the sn-2 acyl groups of membrane phospholipids to release arachidonic acid and lysophospholipids. An acidic phospholipase A2 isolated from Bothrops jararacussu snake venom presents a high catalytic, platelet aggregation inhibition and hypotensive activities. This protein was crystallized in two oligomeric states: monomeric and dimeric. The crystal structures were solved at 1.79 and 1.90 angstroms resolution, respectively, for the two states. It was identified a Na+ ion at the center of Ca2+-binding site of the monomeric form. A novel dimeric conformation with the active sites exposed to the solvent was observed. Conformational states of the molecule may be due to the physicochemical conditions used in the crystallization experiments. We suggest dimeric state is one found in vivo.
==About this Structure==
==About this Structure==
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1U73 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bothrops_jararacussu Bothrops jararacussu]. 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=1U73 OCA].
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1U73 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bothrops_jararacussu Bothrops jararacussu]. 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=1U73 OCA].
==Reference==
==Reference==
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[[Category: Phospholipase A(2)]]
[[Category: Phospholipase A(2)]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Arni, R.K.]]
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[[Category: Arni, R K.]]
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[[Category: Fontes, M.R.]]
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[[Category: Fontes, M R.]]
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[[Category: Magro, A.J.]]
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[[Category: Magro, A J.]]
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[[Category: Murakami, M.T.]]
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[[Category: Murakami, M T.]]
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[[Category: Soares, A.M.]]
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[[Category: Soares, A M.]]
[[Category: acidic phospholipase a2]]
[[Category: acidic phospholipase a2]]
[[Category: bothrops jararacussu venom]]
[[Category: bothrops jararacussu venom]]
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[[Category: x-ray crystallography]]
[[Category: x-ray crystallography]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 03:26:35 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:21:14 2008''

Revision as of 13:21, 21 February 2008


1u73, resolution 1.9Å

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Crystal structure of a Dimeric Acidic Platelet Aggregation Inhibitor and Hypotensive Phospholipase A2 from Bothrops jararacussu

Overview

Phospholipases A2 belong to the superfamily of proteins which hydrolyzes the sn-2 acyl groups of membrane phospholipids to release arachidonic acid and lysophospholipids. An acidic phospholipase A2 isolated from Bothrops jararacussu snake venom presents a high catalytic, platelet aggregation inhibition and hypotensive activities. This protein was crystallized in two oligomeric states: monomeric and dimeric. The crystal structures were solved at 1.79 and 1.90 angstroms resolution, respectively, for the two states. It was identified a Na+ ion at the center of Ca2+-binding site of the monomeric form. A novel dimeric conformation with the active sites exposed to the solvent was observed. Conformational states of the molecule may be due to the physicochemical conditions used in the crystallization experiments. We suggest dimeric state is one found in vivo.

About this Structure

1U73 is a Single protein structure of sequence from Bothrops jararacussu. Active as Phospholipase A(2), with EC number 3.1.1.4 Full crystallographic information is available from OCA.

Reference

Crystal structure of an acidic platelet aggregation inhibitor and hypotensive phospholipase A2 in the monomeric and dimeric states: insights into its oligomeric state., Magro AJ, Murakami MT, Marcussi S, Soares AM, Arni RK, Fontes MR, Biochem Biophys Res Commun. 2004 Oct 8;323(1):24-31. PMID:15351695

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