2fo5
From Proteopedia
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|PDB= 2fo5 |SIZE=350|CAPTION= <scene name='initialview01'>2fo5</scene>, resolution 2.200Å | |PDB= 2fo5 |SIZE=350|CAPTION= <scene name='initialview01'>2fo5</scene>, resolution 2.200Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= EPB2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4513 Hordeum vulgare]) | |GENE= EPB2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4513 Hordeum vulgare]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |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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[[Category: Khosla, C.]] | [[Category: Khosla, C.]] | ||
[[Category: Strop, P.]] | [[Category: Strop, P.]] | ||
| - | [[Category: ACE]] | ||
| - | [[Category: SO4]] | ||
[[Category: cysteine endoprotease]] | [[Category: cysteine endoprotease]] | ||
[[Category: endopeptidase]] | [[Category: endopeptidase]] | ||
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[[Category: leupeptin]] | [[Category: leupeptin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:05:27 2008'' |
Revision as of 00:05, 31 March 2008
| |||||||
| , resolution 2.200Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | EPB2 (Hordeum vulgare) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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
Page seeded by OCA on Mon Mar 31 03:05:27 2008
Categories: Hordeum vulgare | Single protein | Bethune, M T. | Brunger, A T. | Khosla, C. | Strop, P. | Cysteine endoprotease | Endopeptidase | Ep-b2 | Epb | Epb2 | Leupeptin
