1wcg

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[[Image:1wcg.gif|left|200px]]<br />
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[[Image:1wcg.gif|left|200px]]<br /><applet load="1wcg" size="450" color="white" frame="true" align="right" spinBox="true"
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<applet load="1wcg" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1wcg, resolution 1.10&Aring;" />
caption="1wcg, resolution 1.10&Aring;" />
'''APHID MYROSINASE'''<br />
'''APHID MYROSINASE'''<br />
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==About this Structure==
==About this Structure==
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1WCG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Brevicoryne_brassicae Brevicoryne brassicae] with GOL as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Transferred_entry:_3.2.1.147 Transferred entry: 3.2.1.147], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.3.1 3.2.3.1] Structure known Active Site: GLA. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1WCG OCA].
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1WCG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Brevicoryne_brassicae Brevicoryne brassicae] with GOL as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Transferred_entry:_3.2.1.147 Transferred entry: 3.2.1.147], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.3.1 3.2.3.1] Known structural/functional Site: <scene name='pdbsite=GLA:Gol Binding Site For Chain B'>GLA</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1WCG OCA].
==Reference==
==Reference==
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[[Category: thioglucosidase]]
[[Category: thioglucosidase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 17:32:15 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 18:38:21 2007''

Revision as of 16:28, 18 December 2007


1wcg, resolution 1.10Å

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APHID MYROSINASE

Overview

The aphid Brevicoryne brassicae is a specialist feeding on Brassicaceae, plants. The insect has an intricate defence system involving a, beta-D-thioglucosidase (myrosinase) that hydrolyses glucosinolates, sequestered from the host plant into volatile isothiocyanates. These, isothiocyanates act synergistically with the pheromone E-beta-farnesene to, form an alarm system when the aphid is predated. In order to investigate, the enzymatic characteristics of the aphid myrosinase and its, three-dimensional structure, milligram amounts of pure recombinant aphid, myrosinase were obtained from Echerichia coli. The recombinant enzyme had, similar physiochemical properties to the native enzyme. The global, structure is very similar to Sinapis alba myrosinase and plant, beta-O-glucosidases. Aphid myrosinase has two catalytic glutamic acid, residues positioned as in plant beta-O-glucosidases, and it is not obvious, why this unusual enzyme hydrolyses glucosinolates, the common substrates, of plant myrosinases which are normally not hydrolyzed by plant, beta-O-glucosidases. The only residue specific for aphid myrosinase in, proximity of the glycosidic linkage is Tyr180 which may have a catalytic, role. The aglycon binding site differs strongly from plant myrosinase, whereas due to the presence of Trp424 in the glucose binding site, this, part of the active site is more similar to plant beta-O-glucosidases, as, plant myrosinases carry a phenylalanine residue at this position.

About this Structure

1WCG is a Single protein structure of sequence from Brevicoryne brassicae with GOL as ligand. Active as Transferred entry: 3.2.1.147, with EC number 3.2.3.1 Known structural/functional Site: . Full crystallographic information is available from OCA.

Reference

Crystal structure at 1.1 Angstroms resolution of an insect myrosinase from Brevicoryne brassicae shows its close relationship to beta-glucosidases., Husebye H, Arzt S, Burmeister WP, Hartel FV, Brandt A, Rossiter JT, Bones AM, Insect Biochem Mol Biol. 2005 Dec;35(12):1311-20. Epub 2005 Aug 18. PMID:16291087

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