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2fo5

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[[Image:2fo5.gif|left|200px]]<br /><applet load="2fo5" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2fo5.gif|left|200px]]
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caption="2fo5, resolution 2.200&Aring;" />
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'''Crystal structure of recombinant barley cysteine endoprotease B isoform 2 (EP-B2) in complex with leupeptin'''<br />
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{{Structure
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|PDB= 2fo5 |SIZE=350|CAPTION= <scene name='initialview01'>2fo5</scene>, resolution 2.200&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=ACE:ACETYL GROUP'>ACE</scene>
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|ACTIVITY=
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|GENE= EPB2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4513 Hordeum vulgare])
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}}
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'''Crystal structure of recombinant barley cysteine endoprotease B isoform 2 (EP-B2) in complex with leupeptin'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2FO5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Hordeum_vulgare Hordeum vulgare] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=ACE:'>ACE</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FO5 OCA].
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2FO5 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Hordeum_vulgare Hordeum vulgare]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FO5 OCA].
==Reference==
==Reference==
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Heterologous expression, purification, refolding, and structural-functional characterization of EP-B2, a self-activating barley cysteine endoprotease., Bethune MT, Strop P, Tang Y, Sollid LM, Khosla C, Chem Biol. 2006 Jun;13(6):637-47. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16793521 16793521]
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Heterologous expression, purification, refolding, and structural-functional characterization of EP-B2, a self-activating barley cysteine endoprotease., Bethune MT, Strop P, Tang Y, Sollid LM, Khosla C, Chem Biol. 2006 Jun;13(6):637-47. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16793521 16793521]
[[Category: Hordeum vulgare]]
[[Category: Hordeum vulgare]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: leupeptin]]
[[Category: leupeptin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:23:22 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:54:46 2008''

Revision as of 14:54, 20 March 2008

Image:2fo5.gif


PDB ID 2fo5

Drag the structure with the mouse to rotate
, resolution 2.200Å
Ligands: and
Gene: EPB2 (Hordeum vulgare)
Coordinates: save as pdb, mmCIF, xml



Crystal structure of recombinant barley cysteine endoprotease B isoform 2 (EP-B2) in complex with leupeptin


Overview

We describe the heterologous expression in Escherichia coli of the proenzyme precursor to EP-B2, a cysteine endoprotease from germinating barley seeds. High yields (50 mg/l) of recombinant proEP-B2 were obtained from E. coli inclusion bodies in shake flask cultures following purification and refolding. The zymogen was rapidly autoactivated to its mature form under acidic conditions at a rate independent of proEP-B2 concentration, suggesting a cis mechanism of autoactivation. Mature EP-B2 was stable and active over a wide pH range and efficiently hydrolyzed a recombinant wheat gluten protein, alpha2-gliadin, at sequences with known immunotoxicity in celiac sprue patients. The X-ray crystal structure of mature EP-B2 bound to leupeptin was solved to 2.2 A resolution and provided atomic insights into the observed subsite specificity of the endoprotease. Our findings suggest that orally administered proEP-B2 may be especially well suited for treatment of celiac sprue.

About this Structure

2FO5 is a Single protein structure of sequence from Hordeum vulgare. Full crystallographic information is available from OCA.

Reference

Heterologous expression, purification, refolding, and structural-functional characterization of EP-B2, a self-activating barley cysteine endoprotease., Bethune MT, Strop P, Tang Y, Sollid LM, Khosla C, Chem Biol. 2006 Jun;13(6):637-47. PMID:16793521

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