1poc

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(New page: 200px<br /><applet load="1poc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1poc, resolution 2.0&Aring;" /> '''CRYSTAL STRUCTURE OF ...)
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[[Image:1poc.gif|left|200px]]<br /><applet load="1poc" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1poc.gif|left|200px]]<br /><applet load="1poc" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1poc, resolution 2.0&Aring;" />
caption="1poc, resolution 2.0&Aring;" />
'''CRYSTAL STRUCTURE OF BEE-VENOM PHOSPHOLIPASE A2 IN A COMPLEX WITH A TRANSITION-STATE ANALOGUE'''<br />
'''CRYSTAL STRUCTURE OF BEE-VENOM PHOSPHOLIPASE A2 IN A COMPLEX WITH A TRANSITION-STATE ANALOGUE'''<br />
==Overview==
==Overview==
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The 2.0 angstroms crystal structure of a complex containing bee-venom, phospholipase A2 (PLA2) and a phosphonate transition-state analogue was, solved by multiple isomorphous replacement. The electron-density map is, sufficiently detailed to visualize the proximal sugars of the enzyme's, N-linked carbohydrate and a single molecule of the transition-state, analogue bound ot its active center. Although bee-venom PLA2 does not, belong to the large homologous Class I/II family that encompasses most, other well-studied PLA2s, there is segmental sequence similarity and, conservation of many functional substructures. Comparison of the bee-venom, enzyme with other phospholipase structures provides compelling evidence, for a common catalytic mechanism.
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The 2.0 angstroms crystal structure of a complex containing bee-venom phospholipase A2 (PLA2) and a phosphonate transition-state analogue was solved by multiple isomorphous replacement. The electron-density map is sufficiently detailed to visualize the proximal sugars of the enzyme's N-linked carbohydrate and a single molecule of the transition-state analogue bound ot its active center. Although bee-venom PLA2 does not belong to the large homologous Class I/II family that encompasses most other well-studied PLA2s, there is segmental sequence similarity and conservation of many functional substructures. Comparison of the bee-venom enzyme with other phospholipase structures provides compelling evidence for a common catalytic mechanism.
==About this Structure==
==About this Structure==
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1POC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Apis_mellifera Apis mellifera] with CA and GEL 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=1POC OCA].
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1POC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Apis_mellifera Apis mellifera] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=GEL:'>GEL</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=1POC OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Otwinowski, Z.]]
[[Category: Otwinowski, Z.]]
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[[Category: Scott, D.L.]]
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[[Category: Scott, D L.]]
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[[Category: Sigler, P.B.]]
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[[Category: Sigler, P B.]]
[[Category: CA]]
[[Category: CA]]
[[Category: GEL]]
[[Category: GEL]]
[[Category: hydrolase]]
[[Category: hydrolase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:58:13 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:30:50 2008''

Revision as of 12:30, 21 February 2008


1poc, resolution 2.0Å

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CRYSTAL STRUCTURE OF BEE-VENOM PHOSPHOLIPASE A2 IN A COMPLEX WITH A TRANSITION-STATE ANALOGUE

Overview

The 2.0 angstroms crystal structure of a complex containing bee-venom phospholipase A2 (PLA2) and a phosphonate transition-state analogue was solved by multiple isomorphous replacement. The electron-density map is sufficiently detailed to visualize the proximal sugars of the enzyme's N-linked carbohydrate and a single molecule of the transition-state analogue bound ot its active center. Although bee-venom PLA2 does not belong to the large homologous Class I/II family that encompasses most other well-studied PLA2s, there is segmental sequence similarity and conservation of many functional substructures. Comparison of the bee-venom enzyme with other phospholipase structures provides compelling evidence for a common catalytic mechanism.

About this Structure

1POC is a Single protein structure of sequence from Apis mellifera with and as ligands. Active as Phospholipase A(2), with EC number 3.1.1.4 Full crystallographic information is available from OCA.

Reference

Crystal structure of bee-venom phospholipase A2 in a complex with a transition-state analogue., Scott DL, Otwinowski Z, Gelb MH, Sigler PB, Science. 1990 Dec 14;250(4987):1563-6. PMID:2274788

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