2fo5

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[[Image:2fo5.gif|left|200px]]
[[Image:2fo5.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 2fo5 |SIZE=350|CAPTION= <scene name='initialview01'>2fo5</scene>, resolution 2.200&Aring;
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The line below this paragraph, containing "STRUCTURE_2fo5", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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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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|DOMAIN=
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{{STRUCTURE_2fo5| PDB=2fo5 | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2fo5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fo5 OCA], [http://www.ebi.ac.uk/pdbsum/2fo5 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2fo5 RCSB]</span>
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}}
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'''Crystal structure of recombinant barley cysteine endoprotease B isoform 2 (EP-B2) in complex with leupeptin'''
'''Crystal structure of recombinant barley cysteine endoprotease B isoform 2 (EP-B2) in complex with leupeptin'''
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[[Category: Khosla, C.]]
[[Category: Khosla, C.]]
[[Category: Strop, P.]]
[[Category: Strop, P.]]
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[[Category: cysteine endoprotease]]
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[[Category: Cysteine endoprotease]]
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[[Category: endopeptidase]]
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[[Category: Endopeptidase]]
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[[Category: ep-b2]]
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[[Category: Ep-b2]]
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[[Category: epb]]
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[[Category: Epb]]
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[[Category: epb2]]
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[[Category: Epb2]]
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[[Category: leupeptin]]
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[[Category: Leupeptin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 04:07:17 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:05:27 2008''
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Revision as of 01:07, 4 May 2008

Image:2fo5.gif

Template:STRUCTURE 2fo5

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 Page seeded by OCA on Sun May 4 04:07:17 2008

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